IP Library Granted Patent US 12,590,121
Granted Patent B2
US 12,590,121 · App. 17/401,434 · Granted Mar 31, 2026

Peptide compound with repetitive sequences

Inventors: Charlotte A.E. Hauser (Thuwal, SA); Hepi Hari Susapto (Thuwal, SA)
C07K5/101A61L26/0028A61L26/008A61L27/22A61L27/52A61L31/043A61L31/145C08J3/075C08J3/09C12N5/0068A61K38/00C08J2389/00C12N2513/00C12N2533/50
View Patent ↗
Loading inventors, assignments & file history…
Monitor This Case
Get email alerts when status or documents change.
Order Certified Copies
Most orders are placed with the USPTO same day — all within 24 business hours.
Order via The Patent Place →
Pre-filled with this patent's details
Quick Facts
Patent No.
US 12,590,121
App. No.
17/401,434
Granted
Mar 31, 2026
Kind
B2
Abstract

The present disclosure relates to ultrashort peptides capable of forming a gel, to a gel comprising a peptide in accordance with the present disclosure, and to a method of preparing such gel. Such gel is a hydrogel or an organogel. The peptides are suitable bioinks for a bioprinter to build 3D structures through 3D printing as well as other applications.

Claims (244)

1 . An ultrashort peptide consisting of a sequence selected from the group consisting of:

(SEQ ID NO: 2) 

IIFR 

(SEQ ID NO: 3) 

IIFD 

(SEQ ID NO: 4) 

IIFE 

(SEQ ID NO: 5) 

LLFK 

(SEQ ID NO: 6) 

LLFR 

(SEQ ID NO: 7) 

LLFD 

(SEQ ID NO: 8) 

LLFE 

(SEQ ID NO: 9) 

IIZK 

(SEQ ID NO: 10) 

IIZR 

(SEQ ID NO: 11) 

IIZD 

(SEQ ID NO: 12) 

IIZE 

(SEQ ID NO: 13) 

LLZK 

(SEQ ID NO: 14) 

LLZR 

(SEQ ID NO: 15) 

LLZD 

(SEQ ID NO: 16) 

LLZE 

(SEQ ID NO: 17) 

IFFK 

(SEQ ID NO: 18) 

IFFR 

(SEQ ID NO: 19) 

IFFD 

(SEQ ID NO: 20) 

IFFE 

(SEQ ID NO: 21) 

LFFK 

(SEQ ID NO: 22) 

LFFR 

(SEQ ID NO: 23) 

LFFD 

(SEQ ID NO: 24) 

LFFE 

(SEQ ID NO: 25) 

IZZK 

(SEQ ID NO: 26) 

IZZR 

(SEQ ID NO: 27) 

IZZD 

(SEQ ID NO: 28) 

IZZE 

(SEQ ID NO: 29) 

LZZK 

(SEQ ID NO: 30) 

LZZR 

(SEQ ID NO: 31) 

LZZD 

(SEQ ID NO: 32) 

LZZE 

(SEQ ID NO: 33) 

FFIK 

(SEQ ID NO: 34) 

ZZIR 

(SEQ ID NO: 35) 

FFID 

(SEQ ID NO: 36) 

FFIE 

(SEQ ID NO: 37) 

FFLK 

(SEQ ID NO: 38) 

FFLR 

(SEQ ID NO: 39) 

FFLD 

(SEQ ID NO: 40) 

FFLE 

(SEQ ID NO: 41) 

ZZIK 

(SEQ ID NO: 42) 

ZZIR 

(SEQ ID NO: 43) 

ZZID 

(SEQ ID NO: 44) 

ZZIE 

(SEQ ID NO: 45) 

ZZLK 

(SEQ ID NO: 46) 

ZZLR 

(SEQ ID NO: 47) 

ZZLD 

(SEQ ID NO: 48) 

ZZLE 

(SEQ ID NO: 49) 

FIIK 

(SEQ ID NO: 50) 

FIIR 

(SEQ ID NO: 51) 

FIID 

(SEQ ID NO: 52) 

FIIE 

(SEQ ID NO: 53) 

FLLK 

(SEQ ID NO: 55) 

FLLD 

(SEQ ID NO: 56) 

FLLE 

(SEQ ID NO: 57) 

ZIIK 

(SEQ ID NO: 58) 

ZIIR 

(SEQ ID NO: 59) 

ZIID 

(SEQ ID NO: 60) 

ZIIE 

(SEQ ID NO: 61) 

ZLLK 

(SEQ ID NO: 62) 

ZLLR 

(SEQ ID NO: 63) 

ZLLD 

(SEQ ID NO: 64) 

ZLLE 

(SEQ ID NO: 66)

ZZZK,

wherein I is isoleucine, L is leucine, F is phenylalanine, K is lysine, R is arginine, D is aspartic acid, E is glutamic acid, Z is cyclohexylalanine,

wherein each of the sequences is connected to an acetylated or non-acetylated N-terminal protecting group, and may be amidated or non-amidated by a C-terminal protecting group,

wherein the ultrashort peptide is capable of forming a gel by self-assembly,

wherein the N-terminal protecting group is a peptidomimetic molecule,

wherein the N-terminus of the peptidomimetic molecule may be modified with a functional group selected from the group consisting of: carboxylic acid, amide, alcohol, aldehyde, amine, imine, nitrile, an urea analog, phosphate, carbonate, sulfate, nitrate, maleimide, vinyl sulfone, azide, alkyne, alkene, carbohydrate, imide, peroxide, ester, aryl, ketone, sulphite, nitrite, phosphonate, and silane.

2 . The ultrashort peptide recited in claim 1 , wherein the amino acids in the peptide are either L-amino acids or D-amino acids.

3 . The ultrashort peptide recited in claim 1 , wherein the ultrashort peptide is capable of self-assembling into a hydrogel.

4 . The ultrashort peptide recited in claim 1 , wherein the ultrashort peptide is capable of self-assembling into an organogel.

5 . The ultrashort peptide recited in claim 1 , wherein the C-terminal protecting group is selected from the group consisting of: of small molecules, functional groups and linkers.

6 . The ultrashort peptide recited in claim 1 , wherein the C-terminal protecting group is selected from the group consisting of:

polar or non-polar functional groups;

—COOH, —COOR, —COR, —CONHR or —CONRR′ with R and R′ being selected from the group consisting of H, unsubstituted or substituted alkyls, and unsubstituted or substituted aryls;

—NH 2 , —OH, —SH, —CHO, maleimide, imidoester, carbodiimide ester, isocyanate;

small molecules,

comprising sugars, alcohols, hydroxy acids, amino acids, vitamins, or biotin;

linkers terminating in a polar functional group,

comprising ethylenediamine, PEG, carbodiimide ester, or imidoester; and

linkers coupled to small molecules or vitamins,

comprising biotin, sugars, or hydroxy acids.

7 . The ultrashort peptide recited in claim 1 , being stable in aqueous solution at physiological conditions at ambient temperature for a period of time in the range from 1 day to at least 12 months.

8 . A hydrogel comprising the ultrashort peptide recited in claim 1 .

9 . The hydrogel of claim 8 , wherein the hydrogel is stable in aqueous solution at ambient temperature for a period of at least 1 month.

10 . The hydrogel of claim 8 , wherein the hydrogel is characterized by a loss factor tan δ (G″/G′) in the range of 0.08 to 0.17.

11 . The hydrogel of claim 8 , wherein the hydrogel is characterized by a storage modulus G′ from 1250 Pa to 300,000 Pa.

12 . The hydrogel of claim 8 , wherein the hydrogel has a higher mechanical strength than collagen or gelatin.

13 . The hydrogel of claim 8 , wherein the hydrogel is characterized by viscosity in the range of 0.4-0.6 Pa·s.

14 . The hydrogel of claim 8 , comprising fibers of the peptide of claim 1 , the fibers defining a network that is capable of entrapping at least one of a microorganism, a virus particle, a peptide, a peptoid, a protein, a nucleic acid, an oligosaccharide, a polysaccharide, a vitamin, an inorganic molecule, a synthetic polymer, a micro- or nanoparticle, a small organic molecule or a pharmaceutically active compound.

15 . The hydrogel of claim 8 , wherein the hydrogel comprises at least one of a microorganism, a virus particle, a peptide, a peptoid, a protein, a nucleic acid, an oligosaccharide, a polysaccharide, a vitamin, an inorganic molecule, a synthetic polymer, a small organic molecule, a micro- or nanoparticle, or a pharmaceutically active compound entrapped by a network of fibers.

16 . The hydrogel of claim 14 , wherein the fibers are coupled to the at least one of a microorganism, a virus particle, a peptide, a peptoid, a protein, a nucleic acid, an oligosaccharide, a polysaccharide, a vitamin, an inorganic molecule, a synthetic polymer, a small organic molecule, a micro- or nanoparticle, or a pharmaceutically active compound entrapped by the network of fibers.

17 . The hydrogel of claim 8 , wherein the hydrogel is comprised in at least one of a fuel cell, a solar cell, an electronic cell, a biosensing device, a medical device, an implant, a pharmaceutical composition and a cosmetic composition.

18 . The hydrogel of claim 8 , which is injectable.

19 . An organogel comprising the ultrashort peptide recited in claim 1 .

20 . The organogel of claim 19 , wherein the hydrogel is stable in aqueous solution at ambient temperature for a period of at least 1 month.

21 . The organogel of claim 19 , wherein the hydrogel is characterized by a storage modulus G′ from 1250 Pa to 300,000 Pa.

22 . The organogel of claim 19 , wherein the hydrogel has a higher mechanical strength than collagen or gelatin.

23 . The organogel of claim 19 , wherein the hydrogel is characterized by viscosity in the range of 0.4-0.6 Pa·s.

24 . The organogel of claim 19 , comprising fibers of the peptide of claim 1 , the fibers defining a network that is capable of entrapping at least one of a microorganism, a virus particle, a peptide, a peptoid, a protein, a nucleic acid, an oligosaccharide, a polysaccharide, a vitamin, an inorganic molecule, a synthetic polymer, a micro- or nanoparticle, a small organic molecule or a pharmaceutically active compound.

25 . The organogel of claim 19 , wherein the hydrogel comprises at least one of a microorganism, a virus particle, a peptide, a peptoid, a protein, a nucleic acid, an oligosaccharide, a polysaccharide, a vitamin, an inorganic molecule, a synthetic polymer, a small organic molecule, a micro- or nanoparticle, or a pharmaceutically active compound entrapped by a network of fibers.

26 . The organogel of claim 24 , wherein the fibers are coupled to the at least one of a microorganism, a virus particle, a peptide, a peptoid, a protein, a nucleic acid, an oligosaccharide, a polysaccharide, a vitamin, an inorganic molecule, a synthetic polymer, a small organic molecule, a micro- or nanoparticle, or a pharmaceutically active compound entrapped by the network of fibers.

27 . The organogel of claim 19 , wherein the hydrogel is comprised in at least one of a fuel cell, a solar cell, an electronic cell, a biosensing device, a medical device, an implant, a pharmaceutical composition and a cosmetic composition.

28 . The organogel of claim 19 , which is injectable.

29 . A method of preparing a hydrogel or organogel, the method comprising:

dissolving an ultrashort peptide recited in claim 1 in an aqueous solution or an organic solution, respectively.

30 . The method of claim 29 , wherein the dissolved peptide in aqueous or organic solution is further exposed to temperature, wherein the temperature is in the range from 20° C. to 90° C.

31 . The method of claim 29 , wherein the ultrashort peptide is dissolved at a concentration from about 0.01 μg/ml to 100 mg/ml.

32 . The method of claim 29 , wherein the ultrashort peptide is dissolved at a concentration from about 1 mg/ml to 50 mg/ml.

33 . The method of claim 29 , wherein the ultrashort peptide is dissolved at a concentration from about 1 mg/ml to about 20 mg/ml.

34 . A wound dressing or wound healing agent comprising a hydrogel of claim 8 .

35 . A wound dressing or wound healing agent comprising an organogel of claim 19 .

36 . A surgical implant, or stent, the surgical implant or stent comprising a peptide scaffold, wherein the peptide scaffold is formed by a hydrogel of claim 8 .

37 . A surgical implant, or stent, the surgical implant or stent comprising a peptide scaffold, wherein the peptide scaffold is formed by an organogel of claim 19 .

38 . A pharmaceutical composition comprising the ultrashort peptide of claim 1 .

39 . The pharmaceutical composition of claim 38 , further comprising a pharmaceutically active compound.

40 . The pharmaceutical composition of claim 38 , wherein the pharmaceutical composition is provided in the form of a topical gel or cream, a spray, a powder, or a sheet, patch or membrane.

41 . The pharmaceutical composition of claim 38 , wherein the pharmaceutical composition is provided in the form of an injectable solution, a topical gel or cream, a spray, a powder, or a sheet, patch or membrane.

42 . A cosmetic composition comprising the ultrashort peptide of claim 1 .

43 . A biomedical device comprising the ultrashort peptide of claim 1 .

44 . An electronic device comprising the ultrashort peptide of claim 1 .

45 . A kit of parts, the kit comprising a first container with an ultrashort peptide of claim 1 and a second container with an aqueous or organic solution.

46 . The kit of parts of claim 45 , wherein the first container further comprises a pharmaceutically active compound.

47 . The kit of parts of claim 45 , wherein the second container further comprises a pharmaceutically active compound.

48 . The kit of parts of claim 45 , wherein the first container further comprises a pharmaceutically active compound and wherein the second container further comprises a pharmaceutically active compound.

49 . An in vitro or in vivo method of tissue regeneration comprising the steps:

(a) providing a hydrogel of claim 8 ,

(b) exposing the hydrogel to cells which are to form regenerated tissue,

(c) allowing the cells to grow on the hydrogel.

50 . The method of claim 49 , which is performed in vivo, wherein, in step a), the hydrogel is provided at a place in a body where tissue regeneration is intended,

wherein the step a) is performed by injecting the hydrogel at a place in the body where tissue regeneration is intended.

51 . An in vitro or in vivo method of tissue regeneration comprising the steps:

(a) providing an organogel of claim 19 ,

(b) exposing the organogel to cells which are to form regenerated tissue,

(c) allowing the cells to grow on the organogel.

52 . The method of claim 51 , which is performed in vivo, wherein, in step a), the organogel is provided at a place in a body where tissue regeneration is intended,

wherein the step a) is performed by injecting the organogel at a place in the body where tissue regeneration is intended.

53 . A 2D or 3D cell culture substrate comprising a hydrogel of claim 8 .

54 . A 2D or 3D cell culture substrate comprising an organogel of claim 19 .

55 . An ultrashort peptide sequences containing repetitive sequences, the peptide having a general formula selected from:

A n B m X and XB m A n

wherein the total number of amino acids of the ultrashort peptide does not exceed 7 amino acids;

wherein A is an aliphatic amino acids, selected from the group consisting of: isoleucine, leucine or any combination thereof, with n being an integer being selected from 0-5;

wherein B is comprised of at least one aromatic amino acid selected from the group consisting of: tyrosine, tryptophan, phenylalanine, hydrophobic amino acid phenylalanine, or comprised of a peptidomimetic amino acid that is the aliphatic counterpart of the aromatic amino acid;

wherein X is comprised of a polar amino acid, selected from the group consisting of: aspartic acid, glutamic acid, lysine, arginine, histidine, cysteine, serine, threonine, asparagine, and glutamine.

56 . The ultrashort peptide recited in claim 55 , wherein the peptide consists of a sequence selected from the group consisting of:

(SEQ ID NO: 17) 

IFFK 

(SEQ ID NO: 18) 

IFFR 

(SEQ ID NO: 19) 

IFFD 

(SEQ ID NO: 20) 

IFFE 

(SEQ ID NO: 21) 

LFFK 

(SEQ ID NO: 22) 

LFFR 

(SEQ ID NO: 23) 

LFFD 

(SEQ ID NO: 24) 

LFFE 

(SEQ ID NO: 25) 

IZZK 

(SEQ ID NO: 26) 

IZZR 

(SEQ ID NO: 27) 

IZZD 

(SEQ ID NO: 28) 

IZZE 

(SEQ ID NO: 29) 

LZZK 

(SEQ ID NO: 30) 

LZZR 

(SEQ ID NO: 31) 

LZZD 

(SEQ ID NO: 32) 

LZZE 

wherein I is isoleucine, L is leucine, F is phenylalanine, K is lysine, R is arginine, D is aspartic acid, E is glutamic acid, Z is cyclohexylalanine,

wherein each of the sequences may be optionally connected to an acetylated or non-acetylated N-terminal protecting group, and may be amidated or non-amidated by a C-terminal protecting group.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Aug 26, 2021
From: HAUSER, CHARLOTTE A.E.; SUSAPTO, HEPI HARI
To: KING ABDULLAH UNIVERSITY OF SCIENCE AND TECHNOLOGY
Reel/Frame 057293/0964 →
Continuity (2)
Provisional Application 63067913 · Aug 20, 2020
Related Publication 20220056074A1 · Feb 24, 2022
References Cited (367)
US 5445612A · Terakura et al. · 1995 [cited by applicant]
US 8729032B2 · Nagai et al. · 2014 [cited by applicant]
US 10537828B2 · Baxter et al. · 2020 [cited by applicant]
US 20030175410A1 · Campbell et al. · 2003 [cited by applicant]
US 20070154552A1 · Siegal et al. · 2007 [cited by applicant]
US 20080095748A1 · Kharazi et al. · 2008 [cited by applicant]
US 20110008293A1 · Bhandari · 2011 [cited by applicant]
US 20110113053A1 · Khan et al. · 2011 [cited by applicant]
US 20130023460A1 · Hauser et al. · 2013 [cited by applicant]
US 20140012225A1 · Yoo et al. · 2014 [cited by applicant]
US 20140349933A1 · Hauser et al. · 2014 [cited by applicant]
US 20150038428A1 · Hauser et al. · 2015 [cited by applicant]
US 20160136895A1 · Beyer et al. · 2016 [cited by applicant]
US 20160288414A1 · Ozbolat et al. · 2016 [cited by applicant]
US 20160375177A1 · Hauser et al. · 2016 [cited by applicant]
US 20170056548A1 · Lee et al. · 2017 [cited by applicant]
US 20170296760A1 · Lee et al. · 2017 [cited by applicant]
US 20180030501A1 · Bourdeau et al. · 2018 [cited by applicant]
US 20180118978A1 · Yabu et al. · 2018 [cited by applicant]
US 20180361025A1 · Lancaster et al. · 2018 [cited by applicant]
US 20190219572A1 · Mehra et al. · 2019 [cited by applicant]
US 20190321291A1 · Connolly et al. · 2019 [cited by applicant]
US 20200148720A1 · Hauser et al. · 2020 [cited by applicant]
US 20200199514A1 · Hauser et al. · 2020 [cited by applicant]
US 20200247046A1 · Malaquin et al. · 2020 [cited by applicant]
US 20210114276A1 · Nelson et al. · 2021 [cited by applicant]
US 20210121639A1 · Miri Ramsheh et al. · 2021 [cited by applicant]
US 20220054706A1 · Hauser · 2022 [cited by examiner]
US 20220371958A1 · Hauser et al. · 2022 [cited by applicant]
US 20230295225A1 · Hauser · 2023 [cited by examiner]
US 20230405177A1 · Hauser · 2023 [cited by examiner]
CN 105085622A · 2015 [cited by applicant]
CN 105881908A · 2016 [cited by applicant]
CN 109224654A · 2019 [cited by applicant]
CN 111172100A · 2020 [cited by applicant]
EP 0723646B1 · 1996 [cited by applicant]
JP 2005028216A · 2005 [cited by applicant]
JP 2013009598A · 2013 [cited by applicant]
JP 201513850A · 2015 [cited by applicant]
JP 201679190A · 2016 [cited by applicant]
JP 2016530874A · 2016 [cited by applicant]
JP 2017501136A · 2017 [cited by applicant]
JP 2020519605A · 2020 [cited by applicant]
JP 2002320815A · 2020 [cited by applicant]
KR 101596014B1 · 2016 [cited by applicant]
KR 20160091993A · 2016 [cited by applicant]
KR 20190128405A · 2019 [cited by examiner]
KR 1020200007537A · 2020 [cited by applicant]
KR 1020210104339A · 2021 [cited by applicant]
WO 2007102735A1 · 2007 [cited by applicant]
WO 2008057608A1 · 2008 [cited by applicant]
WO WO2008057608A2 · 2008 [cited by examiner]
WO 2012048755A1 · 2012 [cited by applicant]
WO 2013126017A1 · 2013 [cited by applicant]
WO 2014104981A1 · 2014 [cited by applicant]
WO 2014186581A1 · 2014 [cited by applicant]
WO 2014197999A1 · 2014 [cited by applicant]
WO 2015066705A1 · 2015 [cited by applicant]
WO 2015080670A1 · 2015 [cited by applicant]
WO 2015080670A9 · 2015 [cited by applicant]
WO 2015080671A1 · 2015 [cited by applicant]
WO 2016123693A1 · 2016 [cited by applicant]
WO 2016144259A1 · 2016 [cited by applicant]
WO 2016181408A1 · 2016 [cited by applicant]
WO 2017089963A1 · 2017 [cited by applicant]
WO 2018020737A1 · 2018 [cited by applicant]
WO 2018207036A1 · 2018 [cited by applicant]
WO 2018207037A1 · 2018 [cited by applicant]
WO 2020162835A1 · 2020 [cited by applicant]
WO 2021070083A1 · 2021 [cited by applicant]
Feng et al. “Development of a Potent Thrombin Receptor Ligand” J. Med. Chem. 38:4125-4130. (Year: 1995). [cited by examiner]
Thota et al. “Molecular insights into the self-assembly of short amphiphilic peptides FmDn and FmKn” RSC Advances 4:60741 (Year: 2014). [cited by examiner]
Restu et al. “Short Oligopeptides for Biocompatible and Biodegradable Supramolecular Hydrogels” Langmuir 34:8065-8074. (Year: 2018). [cited by examiner]
Chakrobarty et al. “A Self-Healing, All-Organic, Conducting, Composite Peptide Hydrogel as Pressure Sensor and Electrogenic Cell Soft Substrate” ACS Nano 13:163-175. (Year: 2019). [cited by examiner]
Li, Z.; Huang, S.; Liu, Y.; Yao, B.; Hu, T.; Shi, H.; Xie, J.; Fu, X. Scientific Reports 2018, 8, (1), 8020. [cited by applicant]
Jorgensen, W. L.; Tirado-Rives, J. Proceedings of the National Academy of Sciences of the United States of America 2005, 102, (19), 6665. [cited by applicant]
Dodda, L. S.; Cabeza de Vaca, I.; Tirado-Rives, J.; Jorgensen, W. L. Nucleic Acids Research 2017, 45, (W1), W331-W336. [cited by applicant]
Abraham, M. J.; Murtola, T.; Schulz, R.; Páll, S.; Smith, J. C.; Hess, B.; Lindahl, E. SoftwareX 2015, 1-2, 19-25. [cited by applicant]
Darden, T.; York, D.; Pedersen, L. The Journal of Chemical Physics 1993, 98, (12), 10089-10092. [cited by applicant]
Berendsen, H. J. C.; Postma, J. P. M.; Gunsteren, W. F. v.; DiNola, A.; Haak, J. R. The Journal of Chemical Physics 1984, 81, (8), 3684-3690. [cited by applicant]
Bussi, G.; Donadio, D.; Parrinello, M. The Journal of Chemical Physics 2007, 126, (1), 014101. [cited by applicant]
Kim, Y. H.; Baek, N. S.; Han, Y. H.; Chung, M.-A.; Jung, S.-D. Journal of neuroscience methods 2011, 202, (1), 38-44. [cited by applicant]
Riss, T. L.; Valley, M. P.; Zimprich, C. A.; Niles, A. L.; Kupcho, K. R.; Lazar, D. F. 60. Howe, B.; Umrigar, A.; Tsien, F. JoVE (Journal of Visualized Experiments) 2014, (83), e50203. [cited by applicant]
Howe, B.; Umrigar, A.; Tsien, F. JoVE (Journal of Visualized Experiments) 2014, (83), e50203. [cited by applicant]
Worton, R. G.; Duff, C., [27] Karyotyping. In Methods in enzymology, Elsevier: 1979; vol. 58, pp. 322-344. [cited by applicant]
Perrier, A. L.; Tabar, V.; Barberi, T.; Rubio, M. E.; Bruses, J.; Topf, N.; Harrison, N. L.; Studer, L. Proceedings of the National Academy of Sciences 2004, 101, (34), 12543-12548. [cited by applicant]
Kang, J.; Lee, I. Cardiovascular Pathology 2006, 15, (4), 218-221. [cited by applicant]
Blakely, B. D.; Bye, C. R.; Fernando, C. V.; Horne, M. K.; Macheda, M. L.; Stacker, S. A.; Arenas, E.; Parish, C. L. PloS one 2011, 6, (3), e18373. [cited by applicant]
Bowie et al., “Deciphering the Message in Protein Sequences: Tolerance to Amino Acid Substitutions”, Science, vol. 47, pp. 1306-1310 (1990). [cited by applicant]
Burgess et al., “Possible Dissociation of the Heparin-binding Mitogenic Activities of Haparin-binding (Acidic Fibroblast) Growth Factor-1 from Its Receptor-binding Activities by Site-directed Mutagenesis of a Single Lys… [cited by applicant]
Loo et al, “Peptide Bioink: Printable Nanofibrous Scaffolds for 3D Organotyic Cultures”, vol. 15, XP055486589 (2015). [cited by applicant]
Suspato et al, “Ultrashort Peptide Bioinks Support Automated Printing of Large-Scale Constructs Assuring Long-Term Survival of Printed Tissue Constructs”, Nano Lett. 21, 7, pp. 2719-2729 (2021). [cited by applicant]
International Search Report and Written Opinion received in PCT Application No. PCT/IB2021/057622 mailed Dec. 16, 2021. [cited by applicant]
Substantive Examination Report received in Saudi Arabian Application No. 519410522. [cited by applicant]
Fichman et al., “Self-assembly of short peptides to form hydrogels: Design of building blocks, physical properties and technological applications”, Acta Biomaterialia, 16, pp. 1571-1582 (2014). [cited by applicant]
Office Action received in U.S. Appl. No. 16/612,881 mailed May 20, 2021. [cited by applicant]
Office Action received in U.S. Appl. No. 16/612,881 mailed Dec. 30, 2020. [cited by applicant]
Office Action received in Korean Application No. 10-2019-7036272 mailed Oct. 21, 2022. [cited by applicant]
International Search Report and Written Opinion received in PCT Application No. PCT/IB2021/057625 mailed Dec. 14, 2021. [cited by applicant]
International Search Report and Written Opinion received in PCT Application No. PCT/IB2021/057624 mailed Dec. 13, 2021. [cited by applicant]
International Search Report and Written Opinion received in PCT Application No. PCT/IB2021/057623 mailed Dec. 13, 2021. [cited by applicant]
International Search Report and Written Opinion received in PCT Application No. PCT/IB2021/057996 mailed Dec. 20, 2021. [cited by applicant]
International Search Report and Written Opinion received in PCT Application No. PCT/IB2021/057973 mailed Dec. 20, 2021. [cited by applicant]
International Search Report and Written Opinion received in PCT Application No. PCT/IB2021/059652 mailed Feb. 3, 2022. [cited by applicant]
Susapto et al., “Ultrashort Peptide Bioinks Support Automated Printing of Large-Scale Constructs Assuring Long-Term Survival of Printed Tissue Constructs”, Nano Letters, vol. 21, pp. 2719-2729 (2021). [cited by applicant]
Cembran et al., “Biomimetic Materials and Their Utility in Modeling the 3-Dimensional Neural Environment”, iScience, vol. 23, pp. 1-16 (2020). [cited by applicant]
Cunha et al., “3D Culture of adult mouse neural stem cells within functionalized self-assembling peptide scaffolds”, International Journal of Nanomedicine, vol. 6, pp. 943-955 (2011). [cited by applicant]
Marchini et al., “Multi-Functionalized Self-Assembling Peptides as Reproducible 3D Cell Culture Systems Enabling Differentiation and Survival of Various Human Neural Stem Cell Lines”, frontiers in Neuroscience, vol. 14,… [cited by applicant]
Ranjan et al., “A microfiber scaffold-based 3D in vitro human neuronal culture model of Alzheimer's disease”, The Royal Society of Chemistry, vol. 8, pp. 4861-4874 (2020). [cited by applicant]
Alshehri et al., “Scaffolds from Self-Assembling Tetrapeptides Support 3D Spreading, Osteogenic Differentiation, and Angiogenesis of Mesenchymal Stem Cells”, Biomacromolecules, vol. 22, pp. 2094-2106 (2021). [cited by applicant]
Arab, “Novel Nanofibrous Peptide Scaffolds for Tissue Regeneration”, PhD Thesis, Kind Abdullah University of Science and Technology, pp. 1-131 (2019). [cited by applicant]
Ikeno et al., “Effects of self-assembling peptide hydrogel scaffold on bone regeneration with recombinant human bone morphogenetic protein-2”, The International Journal of Oral and Maxillofacial Implants, vol. 28, No. 5… [cited by applicant]
Liu et al., “Stiffness-mediated mesenchymal stem cell fate decision in 3D-bioprinted hydrogels”, Burns and Trauma, vol. 8, pp. 1-13 (2020). [cited by applicant]
Sundararajan et al., “Use of cyanobacterial gas vesicles as oxygen carriers in cell culture”, Cytotechnology, vol. 52, pp. 139-149 (2006). [cited by applicant]
Upadhyay et al., “Understanding Gas Vesicles and Its Scope in Biotechnological Applications”, Advances in Biotechnology and Microbiology, vol. 11, Issue 2, pp. 1-13 (2018). [cited by applicant]
International Search Report and Written Opinion received in PCT Application No. PCT/IB2018/052173 mailed Sep. 9, 2018. [cited by applicant]
International Search Report and Written Opinion received in PCT Application No. PCT/IB2018/052189 mailed Aug. 28, 2018. [cited by applicant]
Office Action received in Saudi Arabian Application No. 519410522. [cited by applicant]
Office Action received in Korean Application No. 10-2019-7036277 mailed Sep. 29, 2021. [cited by applicant]
Office Action received in Saudi Arabian Application No. 519410521. [cited by applicant]
Loo et al., “Peptide Biolink: Self-Assembling Nanofibrous Scaffolds for Three-Dimensional Organotypic Cultures”, Nano Letters, vol. 15, pp. 6919-6925 (2015). [cited by applicant]
Bowie et al., “Deciphering the Message in Protein Sequences: Tolerance of Amino Acid Substitutions”, Science, vol. 247, pp. 1306-1310 (1990). [cited by applicant]
Burgess et al., “Possible Dissociation of the Heparin-binding Mitogenic Activities of Heparin-binding (Acid Fibroblast) Growth Factor-1 from Its Receptor-binding Activities by Site-directed Mutagenesis of a Single Lysin… [cited by applicant]
Loo et al., “Peptide Bioink: Printable Nanofibrous Scaffolds for 3D Organotypic Cultures”, vol. 15, XP055486589 (2015). [cited by applicant]
Fichman et al., “Self-assembly of short peptides to form hydrogels: Design of building blocks, physical properties and technological applications”, Acta Biomaterials, vol. 10, pp. 1671-1682 (2014). [cited by applicant]
Gauthaman, K.; Venugopal, J. R.; Yee, F. C.; Biswas, A.; Ramakrishna, S.; Bongso, A. Osteogenic differentiation of human Wharton's jelly stem cells on nanofibrous substrates in vitro. Tissue Eng., Part A 2011, 17, 71-81. [cited by applicant]
Leng, Q.; Chen, L.; Lv, Y. RNA-based scaffolds for bone regeneration: application and mechanisms of mRNA, miRNA and siRNA. Theranostics 2020, 10, 3190. [cited by applicant]
Erdem, A.; Darabi, M. A.; Nasiri, R.; Sangabathuni, S.; Ertas, Y. N.; Alem, H.; Hosseini, V.; Shamloo, A.; Nasr, A. S.; Ahadian, S. 3D Bioprinting of Oxygenated Cell-Laden Gelatin Methacryloyl Constructs. Adv. Healthcar… [cited by applicant]
Myeroff, C.; Archdeacon, M. Autogenous bone graft: donor sites and techniques. J. Bone Jt. Surg. 2011, 93, 2227-2236. [cited by applicant]
Silbernagel, N.; Körner, A.; Balitzki, J.; Jaggy, M.; Bertels, S.; Richter, B.; Hippler, M.; Hellwig, A.; Hecker, M.; Bastmeyer, M.; Ullrich, N. D. Shaping the Heart: Structural and Functional Maturation of iPSC-Cardiom… [cited by applicant]
Silber, J. S.; Anderson, D. G.; Daffner, S. D.; Brislin, B. T.; Leland, J. M.; Hilibrand, A. S.; Vaccaro, A. R.; Albert, T. J. Donor site morbidity after anterior iliac crest bone harvest for single-level anterior cervi… [cited by applicant]
Alonzo, M.; Alvarez Primo, F.; Anil Kumar, S.; Mudloff, J. A.; Dominguez, E.; Fregoso, G.; Ortiz, N.; Weiss, W. M.; Joddar, B. Bone tissue engineering techniques, advances, and scaffolds for treatment of bone defects. C… [cited by applicant]
Amini, A. R.; Laurencin, C. T.; Nukavarapu, S. P. Bone tissue engineering: recent advances and challenges. Crit. Rev. Biomed. Eng. 2012, 40, 363-408. [cited by applicant]
Bharadwaz, A.; Jayasuriya, A. C. Recent trends in the application of widely used natural and synthetic polymer nanocomposites in bone tissue regeneration. Mater. Sci. Eng., C 2020, 110, No. 110698. [cited by applicant]
Pittenger, M. F.; Mackay, A. M.; Beck, S. C.; Jaiswal, R. K.; Douglas, R.; Mosca, J. D.; Moorman, M. A.; Simonetti, D. W.; Craig, S.; Marshak, D. R. Multilineage potential of adult human mesenchymal stem cells. Science … [cited by applicant]
Ma, K.; Laco, F.; Ramakrishna, S.; Liao, S.; Chan, C. K. Differentiation of bone marrow-derived mesenchymal stem cells into multi-layered epidermis-like cells in 3D organotypic coculture. Biomaterials 2009, 30, 3251-325… [cited by applicant]
Petite, H.; Viateau, V.; Bensaid, W.; Meunier, A.; de Pollak, C.; Bourguignon, M.; Oudina, K.; Sedel, L.; Guillemin, G. Tissue- engineered bone regeneration. Nat. Biotechnol. 2000, 18, 959. [cited by applicant]
Takamine, Y.; Tsuchiya, H.; Kitakoji, T.; Kurita, K.; Ono, Y.; Ohshima, Y.; Kitoh, H.; Ishiguro, N.; Iwata, H. Distraction osteogenesis enhanced by osteoblastlike cells and collagen gel. Clin. Orthop. Relat. Res. 2002, … [cited by applicant]
Kofidis, T.; Lebl, D. R.; Martinez, E. C.; Hoyt, G.; Tanaka, M.; Robbins, R. C. Novel injectable bioartificial tissue facilitates targeted, less invasive, large-scale tissue restoration on the beating heart after myocar… [cited by applicant]
Yildirim, Y.; Naito, H.; Didié, M.; Karikkineth, B. C.; Biermann, D.; Eschenhagen, T.; Zimmermann, W.-H. Development pf a biological ventricular assist device: preliminary data from a small animal model. Circulation 200… [cited by applicant]
Radisic, M.; Park, H.; Shing, H.; Consi, T.; Schoen, F. J.; Langer, R.; Freed, L. E.; Vunjak-Novakovic, G. Functional assembly of engineered myocardium by electrical stimulation of cardiac myocytes cultured on scaffolds… [cited by applicant]
Spadaccio, C.; Chachques, E.; Chello, M.; Covino, E.; Chachques, J. C.; Genovese, J. Predifferentiated adult stem cells and matrices for cardiac cell therapy. Asian Cardiovasc. Thorac. Ann. 2010, 18, 79-87. [cited by applicant]
Kutschka, I.; Chen, I. Y.; Kofidis, T.; Arai, T.; Von Degenfeld, G.; Sheikh, A. Y.; Hendry, S. L.; Pearl, J.; Hoyt, G.; Sista, R.; et al. Collagen matrices enhance survival of transplanted cardiomyoblasts and contribute… [cited by applicant]
Orkin, R.; Gehron, P.; Mcgoodwin, E. B.; Martin, G.; Valentine, T.; Swarm, R. A murine tumor producing a matrix of basement membrane. J. Exp. Med. 1977, 145, 204-220. [cited by applicant]
Sethi, T.; Rintoul, R. C.; Moore, S. M.; Mackinnon, A. C.; Salter, D.; Choo, C.; Chilvers, E. R.; Dransfield, I.; Donnelly, S. C.; Strieter, R.; et al. Extracellular matrix proteins protect small cell lung cancer cells … [cited by applicant]
Grant, D.; Kibbey, M.; Kinsella, J.; Cid, M.; Kleinman, H. The role of basement membrane in angiogenesis and tumor growth. Pathol., Res. Pract. 1994, 190, 854-863. [cited by applicant]
Fushimi, H.; Hiratsuka, T.; Okamura, A.; Ono, Y.; Ogura, I.; Nishimura, I. Recombinant collagen polypeptide as a versatile bone graft biomaterial. Commun. Mater. 2020, 1, No. 1. [cited by applicant]
Kang, P. L.; Huang, H. H.; Chen, T.; Ju, K. C.; Kuo, S. M. Angiogenesis-promoting effect of LIPUS on hADSCs and HUVECs cultured on collagen/hyaluronan scaffolds. Mater. Sci. Eng., C 2019, 102, 22-33. [cited by applicant]
Blokhuis, T.; Arts, J. C. Bioactive and osteoinductive bone graft substitutes: definitions, facts and myths. Injury 2011, 42, S26-S29. [cited by applicant]
Barradas, A.; Yuan, H.; van Blitterswijk, C. A.; Habibovic, P. Osteoinductive biomaterials: current knowledge of properties, experimental models and biological mechanisms. Eur. Cells Mater. 2011, 21, 407-429. [cited by applicant]
Habibovic, P.; de Groot, K. Osteoinductive biomaterials properties and relevance in bone repair. J. Tissue Eng. Regener. Med. 2007, 1, 25-32. [cited by applicant]
Ramier, J.; Grande, D.; Bouderlique, T.; Stoilova, O.; Manolova, N.; Rashkov, I.; Langlois, V.; Albanese, P.; Renard, E. From design of bio-based biocomposite electrospun scaffolds to osteogenic differentiation of human… [cited by applicant]
Adler-Abramovich, L.; Gazit, E. The physical properties of supramolecular peptide assemblies: from building block association to technological applications. Chem. Soc. Rev. 2014, 43, 6881-6893. [cited by applicant]
Biesalski, M. A.; Knaebel, A.; Tu, R.; Tirrell, M. Cell adhesion on a polymerized peptide-amphiphile monolayer. Biomaterials 2006, 27, 1259-1269. [cited by applicant]
Mata, A.; Hsu, L.; Capito, R.; Aparicio, C.; Henrikson, K.; Stupp, S. I. Micropatterning of bioactive self-assembling gels. Soft Matter 2009, 5, 1228-1236. [cited by applicant]
Eren, E. D.; Tansik, G.; Tekinay, A. B.; Guler, M. O. Mineralized peptide nanofiber gels for enhanced osteogenic differentiation. ChemNanoMat 2018, 4, 837-845. [cited by applicant]
Mata, A.; Geng, Y.; Henrikson, K. J.; Aparicio, C.; Stock, S. R.; Satcher, R. L.; Stupp, S. I. Bone regeneration mediated by biomimetic mineralization of a nanofiber matrix. Biomaterials 2010, 31, 6004-6012. [cited by applicant]
Derkus, B.; Okesola, B. O.; Barrett, D. W.; D'Este, M.; Chowdhury, T. T.; Eglin, D.; Mata, A. Multicomponent hydrogels for the formation of vascularized bone-like constructs in vitro. Acta Biomater. 2020, 109, 82-94. [cited by applicant]
Ghosh, M.; Halperin-Sternfeld, M.; Grigoriants, I.; Lee, J.; Nam, K. T.; Adler-Abramovich, L. Arginine-presenting peptide hydrogels decorated with hydroxyapatite as biomimetic scaffolds for bone regeneration. Biomacromo… [cited by applicant]
Tsutsumi, H.; Kawamura, M.; Mihara, H. Osteoblastic differentiation on hydrogels fabricated from Ca2+-responsive self-assembling peptides functionalized with bioactive peptides. Bioorg. Med. Chem. 2018, 26, 3126-3132. [cited by applicant]
Zhang, R.; Liu, Y.; Qi, Y.; Zhao, Y.; Nie, G.; Wang, X.; Zheng, S. Self-assembled peptide hydrogel scaffolds with VEGF and BMP-2 Enhanced in vitro angiogenesis and osteogenesis. Oral Dis. 2021, DOI: 10.1111/odi.13785, i… [cited by applicant]
Misawa, H.; Kobayashi, N.; Soto-Gutierrez, A.; Chen, Y.; Yoshida, A.; Rivas-Carrillo, J. D.; Navarro-Alvarez, N.; Tanaka, K.; Miki, A.; Takei, J.; et al. PuraMatrix facilitates bone regeneration in bone defects of calva… [cited by applicant]
Ikeno, M.; Hibi, H.; Kinoshita, K.; Hattori, H.; Ueda, M. Effects of self-assembling peptide hydrogel scaffold on bone regeneration with recombinant human bone morphogenetic protein-2. Int. J. Oral Maxillofac. Implants … [cited by applicant]
He, B.; Ou, Y.; Chen, S.; Zhao, W.; Zhou, A.; Zhao, J.; Li, H.; Jiang, D.; Zhu, Y. Designer bFGF-incorporated d-form self-assembly peptide nanofiber scaffolds to promote bone repair. Mater. Sci. Eng., C 2017, 74, 451-45… [cited by applicant]
Tsukamoto, J.; Naruse, K.; Nagai, Y.; Kan, S.; Nakamura, N.; Hata, M.; Omi, M.; Hayashi, T.; Kawai, T.; Matsubara, T. Efficacy of a self-assembling peptide hydrogel, SPG-178-gel, for bone regeneration and three-dimensio… [cited by applicant]
Sun, Y.; Li, W.; Wu, X.; Zhang, N.; Zhang, Y.; Ouyang, S.; Song, X.; Fang, X.; Seeram, R.; Xue, W.; He, L.; Wu, W. Functional Self-Assembling Peptide Nanofiber Hydrogels Designed for Nerve Degeneration. ACS Appl. Mater.… [cited by applicant]
Guo, J.; Su, H.; Zeng, Y.; Liang, Y.-X.; Wong, W. M.; Ellis-Behnke, R. G.; So, K.-F.; Wu, W. Reknitting the injured spinal cord by self-assembling peptide nanofiber scaffold. Nanomedicine 2007, 3, 311-321. [cited by applicant]
Liu, X.; Wang, X.; Wang, X.; Ren, H.; He, J.; Qiao, L.; Cui, F.-Z. Functionalized self-assembling peptide nanofiber hydrogels mimic stem cell niche to control human adipose stem cell behavior in vitro. Acta Biomater. 20… [cited by applicant]
Rauf, S.; Susapto, H. H.; Kahin, K.; Alshehri, S.; Abdelrahman, S.; Lam, J. H.; Asad, S.; Jadhav, S.; Sundaramurthi, D.; Gao, X.; Hauser, C. A. E. Self-assembling tetrameric peptides allow in situ 3D bioprinting under p… [cited by applicant]
Susapto, H. H.; Alhattab, D.; Abdelrahman, S.; Khan, Z.; Alshehri, S.; Kahin, K.; Ge, R.; Moretti, M.; Emwas, A.-H.; Hauser, C. A. E. Ultrashort Peptide Bioinks Support Automated Printing of Large-Scale Constructs Assur… [cited by applicant]
Arthur, A.; Zannettino, A.; Gronthos, S. The therapeutic applications of multipotential mesenchymal/stromal stem cells in skeletal tissue repair. J. Cell. Physiol. 2009, 218, 237-245. [cited by applicant]
Polo-Corrales, L.; Latorre-Esteves, M.; Ramirez-Vick, J. E. Scaffold design for bone regeneration. J. Nanosci. Nanotechnol. 2014, 14, 15-56. [cited by applicant]
Holmes, T. C. Novel peptide-based biomaterial scaffolds for tissue engineering. Trends Biotechnol. 2002, 20, 16-21. [cited by applicant]
Hauser, C. A.; Deng, R.; Mishra, A.; Loo, Y.; Khoe, U.; Zhuang, F.; Cheong, D. W.; Accardo, A.; Sullivan, M. B.; Riekel, C.; Ying, J. Y.; Hauser, U. A. Natural tri- to hexapeptides self-assemble in water to amyloid beta… [cited by applicant]
Lei, Y.; Gojgini, S.; Lam, J.; Segura, T. The spreading, migration and proliferation of mouse mesenchymal stem cells cultured inside hyaluronic acid hydrogels. Biomaterials 2011, 32, 39-47. [cited by applicant]
Examination Report received in Saudi Arabian Application No. 519410522 dated Aug. 2, 2022. [cited by applicant]
Search Report and Written Opinion received in PCT Application No. PCT/IB2022/051913 mailed Jun. 14, 2022. [cited by applicant]
Office Action received in U.S. Appl. No. 16/612,580 dated Jun. 6, 2022. [cited by applicant]
Bowie et al., “Deciphering the Message in Protein Sequences: Tolderance to Amino Acid Substitutions”, Science, vol. 249, pp. 1306-1310 (1990). [cited by applicant]
Burgess et al., “Possible dissociation of the heparin-binding and mitogenic activities of heparin-binding (acidic fibroblast) growth factor-1 from its receptor-binding activities by site-directed mutagenesis of a single… [cited by applicant]
Loo et al., “Peptide Bioink: Self-Assembling Nanofibrous Scaffolds for Three-Dimensional Organotypic Cultures”, vol. 15, pp. 1-13, XP055486589 (2015). [cited by applicant]
Gungor-Ozkerim, P. S.; Inci, I.; Zhang, Y. S.; Khademhosseini, A.; Dokmeci, M. R. Biomaterials Science 2018, 6, (5), 915-946. [cited by applicant]
Donderwinkel, I.; van Hest, J. C. M.; Cameron, N. R. Polymer Chemistry 2017, 8, (31), 4451-4471. [cited by applicant]
Gopinathan, J.; Noh, I. Biomater Res 2018, 22, 11-11. [cited by applicant]
Khademhosseini, A.; Camci-Unal, G., 3D Bioprinting in Regenerative Engineering:: Principles and Applications. CRC Press: 2018. [cited by applicant]
Gjorevski, N.; Sachs, N.; Manfrin, A.; Giger, S.; Bragina, M. E.; Ordonez-Moran, P.; Clevers, H.; Lutolf, M. P. Nature 2016, 539, (7630), 560-564. [cited by applicant]
Hauser, C. A. E.; Deng, R.; Mishra, A.; Loo, Y.; Khoe, U.; Zhuang, F.; Cheong, D. W.; Accardo, A.; Sullivan, M. B.; Riekel, C.; Ying, J. Y.; Hauser, U. A. Proceedings of the National Academy of Sciences 2011, 108, (4), … [cited by applicant]
Loo, Y.; Lakshmanan, A.; Ni, M.; Toh, L. L.; Wang, S.; Hauser, C. A. E. Nano Letters 2015, 15, (10), 6919-6925. [cited by applicant]
Seow, W. Y.; Salgado, G.; Lane, E. B.; Hauser, C. A. E. Scientific Reports 2016, 6, 32670. [cited by applicant]
Chan, K. H.; Xue, B.; Robinson, R. C.; Hauser, C. A. E. Scientific Reports 2017, 7, (1), 12897. [cited by applicant]
Wang, H.; Ren, C.; Song, Z.; Wang, L.; Chen, X.; Yang, Z. Nanotechnology 2010, 21, (22), 225606. [cited by applicant]
Raeburn, J.; Pont, G.; Chen, L.; Cesbron, Y.; Levy, R.; Adams, D. J. Soft Matter 2012, 8, (4), 1168-1174. [cited by applicant]
Betush, R. J.; Urban, J. M.; Nilsson, B. L. Peptide Science 2018, 110, (1), e23099. [cited by applicant]
Lakshmanan, A.; Cheong, D. W.; Accardo, A.; Di Fabrizio, E.; Riekel, C.; Hauser, C. A. Proc Natl Acad Sci U S A 2013, 110, (2), 519-24. [cited by applicant]
Bowerman, C. J.; Ryan, D. M.; Nissan, D. A.; Nilsson, B. L. Molecular BioSystems 2009, 5, (9), 1058-1069. [cited by applicant]
Senguen, F. T.; Lee, N. R.; Gu, X.; Ryan, D. M.; Doran, T. M.; Anderson, E. A.; Nilsson, B. L. Molecular BioSystems 2011, 7, (2), 486-496. [cited by applicant]
Surewicz, W. K.; Mantsch, H. H.; Chapman, D. Biochemistry 1993, 32, (2), 389-394. [cited by applicant]
Goormaghtigh, E.; Cabiaux, V.; Ruysschaert, J.-M. European Journal of Biochemistry 1990, 193, (2), 409-420. [cited by applicant]
Williams, R. W.; Dunker, A. K. Journal of Molecular Biology 1981, 152, (4), 783-813. [cited by applicant]
Rivas-Arancibia, S.; Rodríguez-Martínez, E.; Badillo-Ramírez, I.; López-González, U.; Saniger, J. M. Frontiers in Molecular Neuroscience 2017, 10, (137). [cited by applicant]
Seow, W. Y.; Salgado, G.; Lane, E. B.; Hauser, C. A. E. Scientific Reports 2016, 6. [cited by applicant]
Tuncaboylu, D. C.; Argun, A.; Sahin, M.; Sari, M.; Okay, O. Polymer 2012, 53, (24), 5513-5522. [cited by applicant]
Murphy, S. V.; Atala, A. Nature Biotechnology 2014, 32, (8), 773-785. [cited by applicant]
Grinnell, F. Trends in cell biology 2003, 13, (5), 264-269. [cited by applicant]
Franco-Barraza, J.; Beacham, D. A.; Amatangelo, M. D.; Cukierman, E. Current protocols in cell biology 2016, 71, (1), 10.9. 1-10.9. 34. [cited by applicant]
Seliktar, D. Science 2012, 336, (6085), 1124-1128. [cited by applicant]
Baker, B. M.; Chen, C. S. Journal of cell science 2012, 125, (13), 3015-3024. [cited by applicant]
Even-Ram, S.; Yamada, K. M. Current opinion in cell biology 2005, 17, (5), 524-532. [cited by applicant]
Lutolf, M. P.; Lauer-Fields, J. L.; Schmoekel, H. G.; Metters, A. T.; Weber, F. E.; Fields, G. B.; Hubbell, J. A. Proceedings of the National Academy of Sciences 2003, 100, (9), 5413-5418. [cited by applicant]
Mazzeo, M. S.; Chai, T.; Daviran, M.; Schultz, K. M. ACS applied bio materials 2018, 2, (1), 81-92. [cited by applicant]
Discher, D. E.; Mooney, D. J.; Zandstra, P. W. Science 2009, 324, (5935), 1673-1677. [cited by applicant]
Engler, A. J.; Sen, S.; Sweeney, H. L.; Discher, D. E. Cell 2006, 126, (4), 677-689. [cited by applicant]
Chaudhuri, O.; Gu, L.; Klumpers, D.; Darnell, M.; Bencherif, S. A.; Weaver, J. C.; Huebsch, N.; Lee, H.-p.; Lippens, E.; Duda, G. N. Nature materials 2016, 15, (3), 326-334. [cited by applicant]
Dalby, M. J.; Gadegaard, N.; Tare, R.; Andar, A.; Riehle, M. O.; Herzyk, P.; Wilkinson, C. D.; Oreffo, R. O. Nature materials 2007, 6, (12), 997-1003. [cited by applicant]
Haugh, M. G.; Vaughan, T. J.; Madl, C. M.; Raftery, R. M.; McNamara, L. M.; O'Brien, F. J.; Heilshorn, S. C. Biomaterials 2018, 171, 23-33. [cited by applicant]
Silbernagel, N.; Körner, A.; Balitzki, J.; Jaggy, M.; Bertels, S.; Richter, B.; Hippler, M.; Hellwig, A.; Hecker, M.; Bastmeyer, M. Biomaterials 2020, 227, 119551. [cited by applicant]
Darnell, M.; Gu, L.; Mooney, D. Biomaterials 2018, 181, 182-188. [cited by applicant]
Kahin, K.; Khan, Z.; Albagami, M.; Usman, S.; Bahnshal, S.; Alwazani, H.; Majid, M.; Rauf, S.; Hauser, C. In Development of a robotic 3D bioprinting and microfluidic pumping system for tissue and organ engineering, Micr… [cited by applicant]
Mouser, V. H. M.; Melchels, F. P. W.; Visser, J.; Dhert, W. J. A.; Gawlitta, D.; Malda, J. Biofabrication 2016, 8, (3), 035003. [cited by applicant]
Chimene, D.; Peak, C. W.; Gentry, J. L.; Carrow, J. K.; Cross, L. M.; Mondragon, E.; Cardoso, G. B.; Kaunas, R.; Gaharwar, A. K. ACS Applied Materials & Interfaces 2018, 10, (12), 9957-9968. [cited by applicant]
Bertassoni, L. E.; Cardoso, J. C.; Manoharan, V.; Cristino, A. L.; Bhise, N. S.; Araujo, W. A.; Zorlutuna, P.; Vrana, N. E.; Ghaemmaghami, A. M.; Dokmeci, M. R. Biofabrication 2014, 6, (2), 024105. [cited by applicant]
Markstedt, K.; Mantas, A.; Tournier, I.; Martínez Ávila, H. c.; Hagg, D.; Gatenholm, P. Biomacromolecules 2015, 16, (5), 1489-1496. [cited by applicant]
Wilson, S. A.; Cross, L. M.; Peak, C. W.; Gaharwar, A. K. ACS applied materials & interfaces 2017, 9, (50), 43449-43458. [cited by applicant]
Bernal, P. N.; Delrot, P.; Loterie, D.; Li, Y.; Malda, J.; Moser, C.; Levato, R. Advanced materials 2019, 31, (42), 1904209. [cited by applicant]
Kang, H.-W.; Lee, S. J.; Ko, I. K.; Kengla, C.; Yoo, J. J.; Atala, A. Nature biotechnology 2016, 34, (3), 312. [cited by applicant]
Hwang, T. L.; Shaka, A. J. Journal of Magnetic Resonance, Series A 1995, 112, (2), 275-279. 46. Derome, A. E.; Williamson, M. P. Journal of Magnetic Resonance (1969) 1990, 88, (1), 177-185. [cited by applicant]
Piotto, M.; Saudek, V.; Sklenář, V. Journal of Biomolecular NMR 1992, 2, (6), 661-665. 48. Sklenar, V.; Piotto, M.; Leppik, R.; Saudek, V. Journal of Magnetic Resonance, Series A 1993, 102, (2), 241-245. [cited by applicant]
Derome, A. E.; Williamson, M. P. Journal of Magnetic Resonance (1969) 1990, 88, (1), 177-185. [cited by applicant]
Sklenar, V.; Piotto, M.; Leppik, R.; Saudek, V. Journal of Magnetic Resonance, Series A 1993, 102, (2), 241-245. [cited by applicant]
Micsonai, A.; Wien, F.; Kernya, L.; Lee, Y.-H.; Goto, Y.; Réfrégiers, M.; Kardos, J. Proceedings of the National Academy of Sciences 2015, 112, (24), E3095. [cited by applicant]
Maiti, N. C.; Apetri, M. M.; Zagorski, M. G.; Carey, P. R.; Anderson, V. E. Journal of the American Chemical Society 2004, 126, (8), 2399-2408. [cited by applicant]
Loo, Y.; Chan, Y. S.; Szczerbinska, I.; Tan, B. C.; Wan, A. C.; Ng, H. H.; Hauser, C. A. A Chemically Well-Defined, Self-Assembling 3D Substrate for Long-Term Culture of Human Pluripotent Stem Cells. ACS Appl. Bio Mater… [cited by applicant]
Lee, J. H.; Jung, H. W.; Kang, I.-K.; Lee, H. B. Cell behaviour on polymer surfaces with different functional groups. Biomaterials 1994, 15, 705-711. [cited by applicant]
Guo, S.; Zhu, X.; Li, M.; Shi, L.; Ong, J. L. T.; Janćzewski,D.; Neoh, K. G. Parallel Control over Surface Charge and Wettability Using Polyelectrolyte Architecture: Effect on Protein Adsorption and Cell Adhesion. ACS A… [cited by applicant]
Hauser, C. A. E.; Zhang, S. Designer self-assembling peptide nanofiber biological materials. Chem. Soc. Rev. 2010, 39, 2780-2790. [cited by applicant]
Bowerman, C. J.; Ryan, D. M.; Nissan, D. A.; Nilsson, B. L. The Effect of Increasing Hydrophobicity on the Self-Assembly of Amphipathic B-Sheet Peptides. Mol. Biosyst. 2009, 5, 1058-1069. [cited by applicant]
Susapto, H. H.; Alhattab, D.; Abdelrahman, S.; Khan, Z.; Alshehri, S.; Kahin, K.; Ge, R.; Moretti, M.; Emwas, A. H.; Hauser, C. A. E. Ultrashort Peptide Bioinks Support Automated Printing of Large-Scale Constructs Assur… [cited by applicant]
Friedrichs, J.; Taubenberger, A.; Franz, C. M.; Muller, D. J. Cellular Remodelling of Individual Collagen Fibrils Visualized by Time-lapse AFM. J. Mol. Biol. 2007, 372, 594-607. [cited by applicant]
Nakayama, M.; Amano, M.; Katsumi, A.; Kaneko, T.; Kawabata, S.; Takefuji, M.; Kaibuchi, K. Rho-kinase and myosin II activities are required for cell type and environment specific migration. Genes Cells 2005, 10, 107-117. [cited by applicant]
Beadle, C.; Assanah, M. C.; Monzo, P.; Vallee, R.; Rosenfeld, S. S.; Canoll, P. The Role of Myosin II in Glioma Invasion of the Brain. Mol. Biol. Cell 2008, 19, 3357-3368. [cited by applicant]
Friedl, P.; Wolf, K.; Lammerding, J. Nuclear mechanics during cell migration. Curr. Opin. Cell Biol. 2011, 23, 55-64. [cited by applicant]
Balzer, E. M.; Tong, Z.; Paul, C. D.; Hung, W.-C.; Stroka, K. M.; Boggs, A. E.; Martin, S. S.; Konstantopoulos, K. Physical confinement alters tumor cell adhesion and migration phenotypes. FASEB J. 2012, 26, 4045-4056. [cited by applicant]
Khatau, S. B.; Bloom, R. J.; Bajpai, S.; Razafsky, D.; Zang, S.; Giri, A.; Wu, P.-H.; Marchand, J.; Celedon, A.; Hale, C. M.; Sun, S. X.; Hodzic, D.; Wirtz, D. The distinct roles of the nucleus and nucleus-cytoskeleton … [cited by applicant]
Wen, J. H.; Vincent, L. G.; Fuhrmann, A.; Choi, Y. S.; Hribar, K. C.; Taylor-Weiner, H.; Chen, S.; Engler, A. J. Interplay of matrix stiffness and protein tethering in stem cell differentiation. Nat. Mater. 2014, 13, 97… [cited by applicant]
Thievessen, I.; Thompson, P. M.; Berlemont, S.; Plevock, K. M.; Plotnikov, S. V.; Zemljic-Harpf, A.; Ross, R. S.; Davidson, M. W.; Danuser, G.; Campbell, S. L.; Waterman, C. M. Vinculin-actin interaction couples actin r… [cited by applicant]
Humphries, J. D.; Wang, P.; Streuli, C.; Geiger, B.; Humphries, M. J.; Ballestrem, C. Vinculin controls focal adhesion formation by direct interactions with talin and actin. J. Cell. Biol. 2007, 179, 1043-1057. [cited by applicant]
Ode, A.; Schoon, J.; Kurtz, A.; Gaetjen, M.; Ode, J. E.; Geissler, S.; Duda, G. N. CD73/5′-ecto-nucleotidase acts as a regulatory factor in osteo-/chondrogenic differentiation of mechanically stimulated mesenchymal stro… [cited by applicant]
Aslan, H.; Zilberman, Y.; Kandel, L.; Liebergall, M.; Oskouian, R. J.; Gazit, D.; Gazit, Z. Osteogenic differentiation of honcultured immunoisolated bone marrow-derived CD105+ cells. Stem Cells 2006, 24, 1728-1737. [cited by applicant]
Huang, S.; Ingber, D. E. The structural and mechanical complexity of cell-growth control. Nat. Cell Biol. 1999, 1, No. E131. [cited by applicant]
McBeath, R.; Pirone, D. M.; Nelson, C. M.; Bhadriraju, K.; Chen, C. S. Cell shape, cytoskeletal tension, and RhoA regulate stem cell lineage commitment. Dev. Cell 2004, 6, 483-495. [cited by applicant]
Katz, B.-Z.; Zamir, E.; Bershadsky, A.; Kam, Z.; Yamada, K. M.; Geiger, B. Physical state of the extracellular matrix regulates the structure and molecular composition of cell-matrix adhesions. Mol. Biol. Cell 2000, 11,… [cited by applicant]
Cukierman, E.; Pankov, R.; Stevens, D. R.; Yamada, K. M. Taking cell-matrix adhesions to the third dimension. Science 2001, 294, 1708-1712. [cited by applicant]
Fischbach, C.; Kong, H. J.; Hsiong, S. X.; Evangelista, M.B.; Yuen, W.; Mooney, D. J. Cancer cell angiogenic capability is regulated by 3D culture and integrin engagement. Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 399-40… [cited by applicant]
Hsiong, S. X.; Boontheekul, T.; Huebsch, N.; Mooney, D. J. Cyclic arginine-glycine-aspartate peptides enhance three-dimensional stem cell osteogenic differentiation. Tissue Eng., Part A 2009, 15, 263-272. [cited by applicant]
Park, J. S.; Huang, N. F.; Kurpinski, K. T.; Patel, S.; Hsu, S.; Li, S. Mechanobiology of mesenchymal stem cells and their use in cardiovascular repair. Front. Biosci. 2007, 12, 5098-5116. [cited by applicant]
Tan, S.; Fang, J. Y.; Yang, Z.; Nimni, M. E.; Han, B. The synergetic effect of hydrogel stiffness and growth factor on osteogenic differentiation. Biomaterials 2014, 35, 5294-5306. [cited by applicant]
Knight, B.; Laukaitis, C.; Akhtar, N.; Hotchin, N. A.; Edlund, M.; Horwitz, A. R. Visualizing muscle cell migration in situ. Curr. Biol. 2000, 10, 576-585. [cited by applicant]
Roskelley, C.; Desprez, P.; Bissell, M. Extracellular matrix- dependent tissue-specific gene expression in mammary epithelial cells requires both physical and biochemical signal transduction. Proc. Natl. Acad. Sci. U.S.… [cited by applicant]
Thievessen, I.; Fakhri, N.; Steinwachs, J.; Kraus, V.; Mclsaac, R. S.; Gao, L.; Chen, B.-C.; Baird, M. A.; Davidson, M. W.; Betzig, E.; et al. Vinculin is required for cell polarization, migration, and extracellular mat… [cited by applicant]
Case, L. B.; Baird, M. A.; Shtengel, G.; Campbell, S. L.; Hess, H. F.; Davidson, M. W.; Waterman, C. M. Molecular mechanism of vinculin activation and nanoscale spatial organization in focal adhesions. Nat. Cell Biol. 2… [cited by applicant]
Carisey, A.; Ballestrem, C. Vinculin, an adapter protein in control of cell adhesion signalling. Eur. J. Cell Biol. 2011, 90, 157-163. [cited by applicant]
Xu, W.; Baribault, H.; Adamson, E. D. Vinculin knockout results in heart and brain defects during embryonic development. Development 1998, 125, 327-337. [cited by applicant]
Kumar, G.; Tison, C. K.; Chatterjee, K.; Pine, P. S.; McDaniel, J. H.; Salit, M. L.; Young, M. F.; Simon, C. G., Jr. The determination of stem cell fate by 3D scaffold structures through the control of cell shape. Bioma… [cited by applicant]
Pablo Rodriguez, J.; Gonzalez, M.; Rios, S.; Cambiazo, V. Cytoskeletal organization of human mesenchymal stem cells (MSC) changes during their osteogenic differentiation. J. Cell. Biochem. 2004, 93, 721-731. [cited by applicant]
Treiser, M. D.; Yang, E. H.; Gordonov, S.; Cohen, D. M.; Androulakis, I. P.; Kohn, J.; Chen, C. S.; Moghe, P. V. Cytoskeleton-based forecasting of stem cell lineage fates. Proc. Natl. Acad. Sci. U.S.A. 2010, 107, 610-61… [cited by applicant]
Hunter, G. K.; Hauschka, P. V.; Poole, R. A.; Rosenberg, L. C.; Goldberg, H. A. Nucleation and inhibition of hydroxyapatite formation by mineralized tissue proteins. Biochem. J. 1996, 317, 59-64. [cited by applicant]
Wang, J.; Cui, X.; Zhou, Y.; Xiang, Q. Core-shell PLGA/ collagen nanofibers loaded with recombinant FN/CDHs as bone tissue engineering scaffolds. Connect. Tissue Res. 2014, 55, 292-298. [cited by applicant]
Khan, S. N.; Lane, J. M. Bone Tissue Engineering: Basic Science and Clinical Concepts. Orthopedic Tissue Engineering; CRC Press, 2004; pp. 177-194. [cited by applicant]
Oreffo, R. O.; Kusec, V.; Romberg, S.; Triffitt, J. T. Human bone marrow osteoprogenitors express estrogen receptor-alpha and bone morphogenetic proteins 2 and 4 mRNA during osteoblastic differentiation. J. Cell. Bioche… [cited by applicant]
Frank, O.; Heim, M.; Jakob, M.; Barbero, A.; Schafer, D.; Bendik, I.; Dick, W.; Heberer, M.; Martin, I. Real-time quantitative RT-PCR analysis of human bone marrow stromal cells during osteogenic differentiation in vitr… [cited by applicant]
Miron, R.; Zhang, Y. Osteoinduction: a review of old concepts with new standards. J. Dent. Res. 2012, 91, 736-744. [cited by applicant]
Rittling, S. R.; Matsumoto, H. N.; Mckee, M. D.; Nanci, A.; An, X. R.; Novick, K. E.; Kowalski, A. J.; Noda, M.; Denhardt, D. T. Mice lacking osteopontin show normal development and bone structure but display altered os… [cited by applicant]
Chellaiah, M. A.; Kizer, N.; Biswas, R.; Alvarez, U.; Strauss-Schoenberger, J.; Rifas, L.; Rittling, S. R.; Denhardt, D. T.; Hruska, K. A. Osteopontin deficiency produces osteoclast dysfunction due to reduced CD44 surfa… [cited by applicant]
Bax, D. V.; Rodgers, U. R.; Bilek, M. M.; Weiss, A. S. Cell adhesion to tropoelastin is mediated via the C-terminal GRKRK motif and integrin αVβ3. J. Biol. Chem. 2009, 284, 28616-28623. [cited by applicant]
Taddese, S.; Weiss, A. S.; Jahreis, G.; Neubert, R. H.; Schmelzer, C. E. In vitro degradation of human tropoelastin by MMP-12 and the generation of matrikines from domain 24. Matrix Biol. 2009, 28, 84-91. [cited by applicant]
Getie, M.; Schmelzer, C.; Neubert, R. Characterization of peptides resulting from digestion of human skin elastin with elastase. Proteins 2005, 61, 649-657. [cited by applicant]
Phillips, J. E.; Petrie, T. A.; Creighton, F. P.; Garcia, A. J. Human mesenchymal stem cell differentiation on self-assembledmonolayers presenting different surface chemistries. Acta Biomater. 2010, 6, 12-20. [cited by applicant]
Nemir, S.; West, J. L. Synthetic materials in the study of cell response to substrate rigidity. Ann. Biomed. Eng. 2010, 38, 2-20. [cited by applicant]
Holst, J.; Watson, S.; Lord, M. S.; Eamegdool, S. S.; Bax, D. V.; Nivison-Smith, L. B.; Kondyurin, A.; Ma, L.; Oberhauser, A. F.; Weiss, A. S.; Rasko, J. E. J. Substrate elasticity provides mechanical signals for the ex… [cited by applicant]
Rowlands, A. S.; George, P. A.; Cooper-White, J. J. Directing osteogenic and myogenic differentiation of MSCs: interplay of stiffness and adhesive ligand presentation. Am. J. Physiol.: Cell Physiol. 2008, 295, C1037-C10… [cited by applicant]
Saha, K.; Keung, A. J.; Irwin, E. F.; Li, Y.; Little, L.; Schaffer, D. V.; Healy, K. E. Substrate modulus directs neural stem cell behavior. Biophys. J. 2008, 95, 4426-4438. [cited by applicant]
Final Official Action received in Japanese Application No. 2019-561848 dated Oct. 11, 2022. [cited by applicant]
Examination Report received in European Application No. 18 720 665.1 dated Oct. 25, 2022. [cited by applicant]
Official Action received in Japanese Application No. 2019-561747 dated Sep. 13, 2022. [cited by applicant]
Examination Report received in Saudi Arabian Application No. 521430991 dated Aug. 18, 2022. [cited by applicant]
Office Action received in U.S. Appl. No. 16/612,580 dated Sep. 21, 2022. [cited by applicant]
Office Action received in U.S. Appl. No. 17/401,800 dated Aug. 30, 2022. [cited by applicant]
International Search Report and Written Opinion received in International Application No. PCT/IB2022/055194 dated Sep. 20, 2022. [cited by applicant]
International Search Report and Written Opinion received in International Application No. PCT/IB2022/055054 dated Sep. 26, 2022. [cited by applicant]
Chen et al., “Hydrogelation of the Short Self-Assembling Peptide I3QGK Regulated by Transglutaminase and Use for Rapid Hemostasis”, ACS Appl Matter Interfaces, vol. 28, pp. 17833-17841 (2016). [cited by applicant]
Echalier et al., “Modular bioink for 3D printing of biocompatible hydrogels: sol-gel polymerization of hybrid peptides and polymers”, RSC Advances, vol. 7, pp. 12231-12235 (2017). [cited by applicant]
Holzl et al., “Bioink properties before, during and after 3D printing”, Biofabrication, vol. 8, 032002 (2016). [cited by applicant]
Holz et al., “High-Power 365 nm UV LED Mercury Arc Lamp Replacement for Photochemistry and Chemical Photolithography”, ACS Sustainable Chemistry & Engineering, vol. 5, pp. 828-834 (2017). [cited by applicant]
Lim et al., “New Visible-Light Photoinitiating System for Improved Print Fidelity in Gelatin-Based Bioinks”, ACS Biomaterials Science and Engineering, vol. 2, pp. 1752-1762 (2016). [cited by applicant]
Loo et al., “Bioprinting synthetic self-assembling peptide hydrogels for boimedical applications”, Biomedical Materials, vol. 11, No. 1 (2015). [cited by applicant]
Sekine et al., “Capillary Networks for Bio-Artificial Three-Dimensional Tissues Fabricated Using Cell Sheet Based Tissue Engineering”, International Journal of Molecular Sciences, vol. 22, No. 92, pp. 1-12 (2021). [cited by applicant]
Yan et al., “Advances in portable electrospinning devices for in situ delivery of personalized wound care”, Nanoscale, vol. 11, pp. 19166-19178 (2019). [cited by applicant]
Official Action received in Japanese Application No. 2019-561848 dated Feb. 28, 2023. [cited by applicant]
Decision of Dismissal of Amendment received in Japanese Application No. 2019-561747 mailed Apr. 18, 2023. [cited by applicant]
Office Action received in U.S. Appl. No. 17/401,800 mailed Apr. 11, 2022. [cited by applicant]
Huebsch, N.; Arany, P. R.; Mao, A. S.; Shvartsman, D.; Ali, O. A.; Bencherif, S. A.; Rivera-Feliciano, J.; Mooney, D. J. Harnessing traction-mediated manipulation of the cell/matrix interface to control stem-cell fate. … [cited by applicant]
Kabiri, K.; Omidian, H.; Hashemi, S.; Zohuriaan-Mehr, M. Synthesis of fast-swelling superabsorbent hydrogels: effect of cross-linker type and concentration on porosity and absorption rate. Eur. Polym. J. 2003, 39, 1341-… [cited by applicant]
Hale, B. W.; Goodrich, L. R.; Frisbie, D. D.; Mcllwraith, C. W.; Kisiday, J. D. Effect of scaffold dilution on migration of mesenchymal stem cells from fibrin hydrogels. Am. J. Vet. Res. 2012, 73, 313-318. [cited by applicant]
Cuchiara, M. P.; Allen, A. C.; Chen, T. M.; Miller, J. S.; West, J. L. Multilayer microfluidic PEGDA hydrogels. Biomaterials 2010, 31, 5491-5497. [cited by applicant]
Cheng, R.; Yan, Y.; Liu, H.; Chen, H.; Pan, G.; Deng, L.; Cui, W. Mechanically enhanced lipo-hydrogel with controlled release of multi-type drugs for bone regeneration. Appl. Mater. Today 2018, 12, 294-308. [cited by applicant]
Engler, A. J.; Sen, S.; Sweeney, H. L.; Discher, D. E. Matrix elasticity directs stem cell lineage specification. Cell 2006, 126, 677-689. [cited by applicant]
Sivaraj, K. K.; Adams, R. H. Blood vessel formation and function in bone. Development 2016, 143, 2706-2715. [cited by applicant]
Kim, S.; Cha, C. Enhanced mechanical and electrical properties of heteroscaled hydrogels infused with aqueous-dispersible hybrid nanofibers. Biofabrication 2020, 12, No. 015020. [cited by applicant]
Hwang, T. L.; Shaka, A. J., Water Suppression That Works. Excitation Sculpting Using Arbitrary Wave-Forms and Pulsed-Field Gradients. J. Magn. Reson. 1995, 112, (2), 275-279. [cited by applicant]
Derome, A. E.; Williamson, M. P., Rapid-Pulsing Artifacts in Double-Quantum-Filtered COSY. J. Magn. Reson. 1990, 88, (1), 177-185. [cited by applicant]
Piotto, M.; Saudek, V.; Sklenář, V., Gradient-Tailored Excitation for Single-Quantum NMR Spectroscopy of Aqueous Solutions. J. Biomol. NMR 1992, 2, (6), 661-665. [cited by applicant]
Sklenar, V.; Piotto, M.; Leppik, R.; Saudek, V., Gradient-Tailored Water Suppression for 1H-15N HSQC Experiments Optimized to Retain Full Sensitivity. J. Magn. Reson. 1993, 102, (2), 241-245. [cited by applicant]
Gilbert, D. F.; Erdmann, G.; Zhang, X.; Fritzsche, A.; Demir, K.; Jaedicke, A.; Muehlenberg, K.; Wanker, E. E.; Boutros, M., A novel multiplex cell viability assay for high-throughput RNAi screening. PloS One 2011, 6, (… [cited by applicant]
Arab, “Novel Nanofibrous Peptide Scaffolds for Tissue Regeneration”, Dissertation, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia, Apr. 2019. [cited by applicant]
Ikeno et al., “Effects of self-assembling peptide hydrogel scaffold on bone regeneration with recombinant human bone morphogenetic protein-2”; The International Journal of Oral and Maxillofacial Implants; vol. 28, No. 5… [cited by applicant]
Liu et al., “Stiffness-mediated mesenchymal stem cell fate decision in 3D-bioprinted hydrogels”; Burns & Trauma, vol. 8, pp. 1-13 (2020). [cited by applicant]
International Search Report and Written Opinion received in International Application No. PCT/IB2021/057623 mailed Dec. 13, 2021. [cited by applicant]
Office Action received in Japanese Patent Application No. 2019-561848 mailed Apr. 5, 2022. [cited by applicant]
Office Action received in Japanese Patent Application No. 2019-561747 mailed Mar. 15, 2022. [cited by applicant]
Notice of Allowance received in Korean Application No. 10-2019-7036377 dated Apr. 6, 2022. [cited by applicant]
Search Report and Written Opinion received in PCT Application No. PCT/IB2021/060795. [cited by applicant]
Ali et al., “A Non-Canonical NRPS Is Involved in the Synthesis of Fungisporin and Related Hydrophobic Cyclic Tetrapeptides in Penicillium chrysogenum”, PLOS ONE, vol. 9, Issue 6, pp. 1-10 (2014). [cited by applicant]
Alrashoudi et al., “Fabrication of a Lateral Flow Assay for Rapid In-Field Detection of COVID-19 Antibodies Using Additive Manufacturing Printing Technologies”, International Journal of Bioprinting, vol. 7, Issue 4, pp.… [cited by applicant]
Farrera-Soler et al, “Identification of immunodominant linear epitodes from SARS-CoV-2 patient plasma”, PLOS ONE, pp. 1-15 (2020). [cited by applicant]
Saatci, Newly developed methods for SARS-CoV-2 detection [SARS-CoV-2 saptanmasinda yeni gelistririlen tani yontemleri], Turk J. Biochem., 45 (5), pp. 465-474 (2020). [cited by applicant]
Vasco et al., “Macrocyclization of Peptide Side Chains by the Ugi Reaction: Achieving Peptide Folding and Exocyclic N-Functionalization in One Shot”, Journal of Organic Chemistry, 80, pp. 6697-6707 (2015). [cited by applicant]
Xiang et al., “A novel double antibody sandwich-lateral flow immunoassay for the rapid and simple detection of hepatitis C virus”, International Journal of Molecular Medicine, 30, pp. 1041-1047 (2012). [cited by applicant]
Examination Report received in European Patent Application No. 18 718 922.0 dated May 20, 2022. [cited by applicant]
Written Opinion received in Singapore Application No. 10202112455P dated Jul. 11, 2023. [cited by applicant]
Office Action received in Japanese Application No. 2019-561848 dated May 22, 2023. [cited by applicant]
Notice of Final Rejection received in Korean Application No. 10-2019-7036272 dated May 25, 2023. [cited by applicant]
European Search Report received in European Application No. 23159765.9 dated Jun. 22, 2023. [cited by applicant]
Ali et al., “A Non-Canonical NRPS Is Involved in the Synthesis of Fungisporin and Related Hydrophobic Cyclic Tetrapeptides in Penicillium chrysogenum”, PLOS ONE; vol. 9, Issue 6, e98212 (2014). [cited by applicant]
Pubchem CID: 93078 “L-Aspartyl-L_phenylalanine” (2005). [cited by applicant]
Vasco et al., “Macrocyclization of Peptide Side Chains by the Ugi Reaction: Achieving Peptide Folding and Exocyclic N-Functionalization in One Shot”, The Journal of Organic Chemistry, 80, pp. 6697-6707 (2015). [cited by applicant]
Zhang et al., “Catechol functionalized hyperbranched polymers as biomedical materials”, Polymers in Polymer Science, vol. 78, pp. 47-55 (2018). [cited by applicant]
Examination Report received in Saudi Arabian Application No. 523442624 mailed Sep. 28, 2023. [cited by applicant]
International Search Report and Written Opinion received in PCT Application No. PCT/IB2023/056328 mailed Oct. 13, 2023. [cited by applicant]
Liu et al., “Stiffness-mediated mesenchymal stem cell fate decision in 3D-bioprinted hydrogels”, Burns & Trauma, vol. 8 (2020). [cited by applicant]
Written Opinion received in Singapore Application No. 1020112455P dated Mar. 27, 2024. [cited by applicant]
Examination Report received in Saudi Arabian Application No. 523442596 dated Mar. 31, 2024. [cited by applicant]
Non-Final Office Action received in U.S. Appl. No. 18/021,645 dated Apr. 1, 2024. [cited by applicant]
Pubchem CID: 97078 “L-Aspartyl-L-phenylalanine”. [cited by applicant]
Extended European Search Report received in European Application No. 21857887.0 dated Sep. 23, 2024. [cited by applicant]
Arab et al., “Evaluation of peptide nanogels for accelerated wound healing in normal micropigs”, Frontiers in Nanoscience and Nanotechnology, vol. 4, pp. 1-9 (2018). [cited by applicant]
Arab, “Novel Nanofibrous Peptide Scaffolds for Tissue Regeneration”, PhD Thesis, XP055901075 (2019). [cited by applicant]
Ceylan et al., “Mussel Inspired Dynamic Cross-Linking of Self-Healing Peptide Nanofiber Network”, Advanced Functional Materials, vol. 23, pp. 2081-2090 (2013). [cited by applicant]
Chakraborty et al., “A Self-Healing, All-Organic, Conducting, Composite Peptide Hydrogel as Pressure Sensor and Electrogenic Cell Soft Substrate”, ACS Nano, vol. 13, pp. 163-175 (2019). [cited by applicant]
Cringoli et al., “Bioadhesive supramolecular hydrogel from unprotected short D,L-peptides with Phe-Phe and Leu-Asp-Val motifs”, Royal Society of Chemistry, vol. 56, pp. 3015-2018 (2020). [cited by applicant]
Dooley et al., “Selective Ligands for the u, S, and x Opiod Receptors Identified from a Single Mixture Based Tetrapeptide Positional Scanning Combinatorial Library”, The Journal of Biological Chemistry, vol. 278, No. 30… [cited by applicant]
Duncan et al., “Short Peptides in Minimalistic Biocatalyst Design”, Biocatalysis, No. 1, pp. 67-81 (2015). [cited by applicant]
Extended European Search Report received in European Application No. 21863813.8 dated Sep. 9, 2024. [cited by applicant]
Extended European Search Report received in European Application No. 21857886.2 dated Jul. 29, 2024. [cited by applicant]
Extended European Search Report received in European Application No. 21882283.1 dated Sep. 16, 2024. [cited by applicant]
Feng et al., “Development of a Potent Thrombin Receptor Ligand”, J. Med. Chem., vol. 38, pp. 4125-4130 (1995). [cited by applicant]
Final Office Action received in U.S. Appl. No. 17/401,434 dated Jul. 17, 2024. [cited by applicant]
Lee et al., “Enzyme-crosslinked gene-activated matrix for the induction of mesenchymal stem cells in osteochondral tissue regeneration”, Acta Biomaterialia, vol. 63, pp. 210-226 (2017). [cited by applicant]
Li et al., “Peptide-Templated Synthesis of TiO2, Nanofibers with Tunable Photocatalytic Activity”, Chem. Eur. J., vol. 24, pp. 18123-18129 (2018). [cited by applicant]
Liu et al., “Stiffness-mediated mesenchymal stem cell fate decision in 3D-bioprinted hydrogels”, Burns & Trauma, vol. 8, tkaa029 (2020). [cited by applicant]
Nakatsu et al., “An Optimized Three-Dimensional In Vitro Model for the Analysis of Angiogenesis”, Methods in Enzymology, vol. 443, pp. 65-82 (2008). [cited by applicant]
Ramirez-Calderon et al., “Delivery of Endothelial Cell-Laden Microgel Elicits Angiogenesis in Self-Assembling Ultrashort Peptide Hydrogels in Vitro”, ACS Appl. Mater. Interfaces, vol. 13, pp. 29281-29292 (2021). [cited by applicant]
Restu et al., “Short Oligopeptides for Biocompatible and Biodegradeable Supremolecular Hydrogels”, Langmuir, vol. 34, pp. 8065-8074 (2018). [cited by applicant]
Notification of the Substantive Examination Report received in Saudi Arabian Application No. 523440449 dated Aug. 27, 2024. [cited by applicant]
Shin et al., “The position of lysine controls the catechol-mediated surface adhesion and cohesion in underwater mussel adhesion”, Journal of Colloid and Interface science, vol. 563, pp. 168-176 (2020). [cited by applicant]
Thota et al. “Molecular insights into the self-assembly of short amphiphilic peptides FmDn and FmKn”, RSC Adv., vol. 4, pp. 60/41-60/48 (2014). [cited by applicant]
Written Opinion received in Singaporean Application No. 10202112428Y dated Sep. 18, 2024. [cited by applicant]
Zhang et al., “Compatability of Neural Stem Cells with Functionalized Self-assembling Peptide Scaffold In vitro”, Biotechnology and Bioprocess Engineering, vol. 15, pp. 545-551 (2010). [cited by applicant]