Granted Patent
B2
US 12,357,965 · App. 18/460,024 · Granted Jul 15, 2025
Supramolecular filamentous assemblies for protein purification
Inventors:
Honggang Cui (Lutherville, MD); Yi Li (Baltimore, MD); Lye Lin Lock (Maynard, MA); XuanKuo Xu (Boxborough, MA); Zhengjian Li (Sudbury, MA)
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Abstract
The present invention provide novel immunofiber compositions for protein or peptide purification and simple and cost-efficient methods and systems using these compositions. In some embodiments, the immunofibers comprise a customized Z-33 peptide derived from Staphylococcus aureus Protein A which is used to construct immuno-amphiphile molecules that assemble into immunofibers in aqueous solution with bioactive epitopes on the surface and have peptide or protein binding ability.
Claims (21)
1. An immunofiber composition comprising:
a) a spacer molecule having a hydrocarbon chain at its N-terminus conjugated to a peptide sequence comprising the generic amino acid sequence of XXBB,
wherein XX is two amino acids having a small hydrophobic side chain and can be the same or different amino acid, and
wherein BB is two amino acids having a negatively charged side chain and can be the same or different amino acid; and
b) an immunofiber binding molecule comprising an antibody binding peptide conjugated to a second hydrocarbon chain,
wherein the antibody binding peptide has a hydrophilic amino acid sequence selected from the group consisting of SEQ ID NOS: 1-7.
2. The immunofiber composition of claim 1 , wherein each of the amino acids having a small hydrophobic side chain is independently selected from the group consisting of: Ala, Val, Ile, and Leu.
3. The immunofiber composition of claim 1 , wherein each of the amino acids having a negatively charged side chain is independently selected from the group consisting of: Glu and Asp.
4. The immunofiber composition of claim 1 , wherein XXBB is VVEE (SEQ ID NO: 10).
5. The immunofiber composition of claim 1 , wherein the hydrocarbon chain is a C12 hydrocarbon chain.
6. The immunofiber composition of claim 1 , wherein the antibody binding peptide has the amino acid sequence FNMQQQRRFYEALHDPNLNEEQRNAKIKSIRDD (SEQ ID NO: 1).
7. The immunofiber composition of claim 1 , wherein the second hydrocarbon chain is between 8 and 22 carbons in length and is either linear or branched.
8. The immunofiber composition of claim 1 , wherein the second hydrocarbon chain is between 8 and 12 carbons in length.
9. A method for purifying antibodies or Fc-containing peptides or proteins, said method comprising:
a) dissolving the immunofiber composition of claim 1 in an aqueous solution at a physiological pH to provide an immunofiber solution and aging the immunofiber solution overnight to provide a solution of self-assembled immunofibers;
b) mixing a sample comprising antibodies or Fc-containing peptides or proteins with the solution of self-assembled immunofibers to provide a solution comprising immunofiber/antibody complexes or immunofiber/Fc-containing peptide or protein complexes;
c) separating the immunofiber/antibody complexes or the immunofiber/Fc-containing peptide or protein complexes from the solution by adding salt and centrifuging; and
d) dissociating the immunofibers from the antibodies or Fc-containing peptide or protein complexes and collecting the unbound antibodies or Fc-containing peptides or proteins.
10. The method of claim 9 , wherein aging the immunofiber solution overnight promotes binding of the immunofibers to the Fc portions of the antibodies or Fc-containing peptides or proteins.
11. The method of claim 9 , wherein dissociating the immunofibers from the antibodies or Fc-containing peptides or proteins comprises lowering the pH to an elution condition; and using one or more of filtration, microfiltration, or ultrafiltration.
12. The method of claim 9 , further comprising further purifying the antibodies or Fc-containing peptides or proteins using polishing.
Assignments (3)
ASSIGNMENT OF ASSIGNOR'S INTEREST
Recorded Dec 4, 2023
From: CUI, HONGGANG; LI, YI
To: THE JOHNS HOPKINS UNIVERSITY
Reel/Frame 065747/0740 →
ASSIGNMENT OF ASSIGNOR'S INTEREST
Recorded Dec 4, 2023
From: LI, ZHENGJIAN; XU, XUANKUO; LOCK, LYE LIN
To: BRISTOL-MYERS SQUIBB COMPANY
Reel/Frame 065747/0746 →
ASSIGNMENT OF ASSIGNOR'S INTEREST
Recorded Dec 4, 2023
From: LI, ZHENGJIAN; XU, XUANKUO; LOCK, LYE LIN
To: BRISTOL-MYERS SQUIBB COMPANY
Reel/Frame 065756/0648 →
Continuity (3)
Division
16639763
Provisional Application
62547256
· Aug 18, 2017
References Cited (172)
US 5223409A
· Ladner et al.
· 1993
[cited by applicant]
US 5403484A
· Ladner et al.
· 1995
[cited by applicant]
US 5427908A
· Dower et al.
· 1995
[cited by applicant]
US 5476996A
· Wilson et al.
· 1995
[cited by applicant]
US 5545806A
· Lonberg et al.
· 1996
[cited by applicant]
US 5545807A
· Surani et al.
· 1996
[cited by applicant]
US 5569825A
· Lonberg et al.
· 1996
[cited by applicant]
US 5571698A
· Ladner et al.
· 1996
[cited by applicant]
US 5580717A
· Dower et al.
· 1996
[cited by applicant]
US 5625126A
· Lonberg et al.
· 1997
[cited by applicant]
US 5633425A
· Lonberg et al.
· 1997
[cited by applicant]
US 5661016A
· Lonberg et al.
· 1997
[cited by applicant]
US 5698767A
· Wilson et al.
· 1997
[cited by applicant]
US 5770429A
· Lonberg et al.
· 1998
[cited by applicant]
US 5789650A
· Lonberg et al.
· 1998
[cited by applicant]
US 5814318A
· Lonberg et al.
· 1998
[cited by applicant]
US 5874299A
· Lonberg et al.
· 1999
[cited by applicant]
US 5877397A
· Lonberg et al.
· 1999
[cited by applicant]
US 5885793A
· Griffiths et al.
· 1999
[cited by applicant]
US 5939598A
· Kucherlapati et al.
· 1999
[cited by applicant]
US 5969108A
· McCafferty et al.
· 1999
[cited by applicant]
US 6013763A
· Braisted et al.
· 2000
[cited by applicant]
US 6075181A
· Kucherlapati et al.
· 2000
[cited by applicant]
US 6114598A
· Kucherlapati et al.
· 2000
[cited by applicant]
US 6150584A
· Kucherlapati et al.
· 2000
[cited by applicant]
US 6162963A
· Kucherlapati et al.
· 2000
[cited by applicant]
US 6172197B1
· McCafferty et al.
· 2001
[cited by applicant]
US 6197927B1
· Braisted
· 2001
[cited by applicant]
US 6521404B1
· Griffiths et al.
· 2003
[cited by applicant]
US 6544731B1
· Griffiths et al.
· 2003
[cited by applicant]
US 6555313B1
· Griffiths et al.
· 2003
[cited by applicant]
US 6582915B1
· Griffiths et al.
· 2003
[cited by applicant]
US 6593081B1
· Griffiths et al.
· 2003
[cited by applicant]
US 6641816B1
· Chevalier
· 2003
[cited by examiner]
US 8076295B2
· Hulvat
· 2011
[cited by applicant]
US 9650421B2
· Stupp
· 2017
[cited by applicant]
US 20090098652A1
· Stupp et al.
· 2009
[cited by applicant]
US 20130101628A1
· Webber et al.
· 2013
[cited by applicant]
US 20180221513A1
· Preslar
· 2018
[cited by examiner]
JP 2020512385
· 2020
[cited by applicant]
WO WO199203918
· 1992
[cited by applicant]
WO WO199312227
· 1993
[cited by applicant]
WO WO199425585
· 1994
[cited by applicant]
WO WO199713852
· 1997
[cited by applicant]
WO WO199824884
· 1998
[cited by applicant]
WO WO199945962
· 1999
[cited by applicant]
WO WO200114424
· 2001
[cited by applicant]
WO WO2002243478
· 2002
[cited by applicant]
WO WO2017123585
· 2017
[cited by applicant]
WO WO2018183417
· 2018
[cited by applicant]
Altunbas et al., Encapsulation of curcumin in self-assembling peptide hydrogels as injectable drug delivery vehicles. Biomaterials 2011, 32 (25), 5906-14.
[cited by applicant]
Arslan, et al., Bioactive supramolecular peptide nanofibers for regenerative medicine. Advanced healthcare materials 2014, 3, (9), 1357-1376.
[cited by applicant]
Bellomo, et al., Stimuli-responsive polypeptide vesicles by conformation-specific assembly. Nat Mater 2004, 3, (4), 244-8.
[cited by applicant]
Benzinger, et al., Propagating structure of Alzheimer's beta-amyloid (10-35) is parallel beta-sheet with residues in exact register. Proc. Natl. Acad. Sci. U. S. A. 1998, 95, (23), 13407-13412.
[cited by applicant]
Biancalana, et al., Molecular mechanism of Thioflavin-T binding to amyloid fibrils. Biochim Biophys Acta 2010, 1804, (7), 1405-12.
[cited by applicant]
Bitton, et al., Self-assembly of model DNA-binding peptide amphiphiles. Langmuir 2005, 21, (25), 11888-11895.
[cited by applicant]
Black et al., Self-Assembled Peptide Amphiphile Micelles Containing a Cytotoxic T-Cell Epitope Promote a Protective Immune Response In Vivo. Adv Mater 2012, 24 (28), 3845-3849.
[cited by applicant]
Boutelje et al., Human immunodeficiency viral protease is catalytically active as a fusion protein: characterization of the fusion and native enzymes produced in
[cited by applicant]
Braisted, et al., Minimizing a binding domain from protein A. Proceedings of the National Academy of Sciences 1996, 93, (12), 5688-5692.
[cited by applicant]
Cheetham, et al., Supramolecular nanostructures formed by anticancer drug assembly. J Am Chem Soc 2013, 135, (8), 2907-10.
[cited by applicant]
Chen et al. Immunoglobulin gene rearrangement in B cell deficient mice generated by targeted deletion of the JH locus (1993) International Immunology 5: 647-656.
[cited by applicant]
Chen et al., B cell development in mice that lack one or both immunoglobulin kappa light chain genes. (1993) EMBO J. 12: 821-830.
[cited by applicant]
Choi et al., Transgenic mice containing a human heavy chain immunoglobulin gene fragment cloned in a yeast artificial chromosome (1993) Nature Genetics 4:117-123.
[cited by applicant]
Chothia, et al., Helix to helix packing in proteins. J. Mol. Biol. 1981, 145, (1), 215-250.
[cited by applicant]
Chow et al., Self-assembling nanostructures to deliver angiogenic factors to pancreatic islets. Biomaterials 2010, 31 (24), 6154-61.
[cited by applicant]
Chu-Kung, et al., Effect of Fatty Acid Conjugation on Antimicrobial Peptide Activity; DTIC Document: 2004.
[cited by applicant]
Clackson et al., Making antibody fragments using phage display libraries., Nature 352:624-628 (1991).
[cited by applicant]
Cuatrecasas., Protein purification by affinity chromatography. J. Biol. Chem 1970, 245 (12), 3050.
[cited by applicant]
Cui et al., Amino Acid Sequence in Constitutionally Isomeric Tetrapeptide Amphiphiles Dictates Architecture of One-Dimensional Nanostructures. Journal of the American Chemical Society 2014, 136 (35), 12461-12468.
[cited by applicant]
Cui, et al., Self-assembly of peptide amphiphiles: from molecules to nanostructures to biomaterials. Biopolymers 2010, 94, (1), 1-18.
[cited by applicant]
Deisenhofer., Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from
[cited by applicant]
Demers et al., Binding mechanism of an SH3 domain studied by NMR and ITC. Journal of the American Chemical Society 2009, 131 (12), 4355-4367.
[cited by applicant]
Deng et al. Self-assembly of Peptide-Amphiphile C12-Abeta (I 1-17) into Nanofibrils. Journal of Physical Chemistry B. 2009, vol. 113, No. 25, pp. 8539-8544. (Year: 2009).
[cited by applicant]
Ecker et al., The therapeutic monoclonal antibody market. MAbs 2015, 7 (1), 9-14.
[cited by applicant]
Eisen et al., Variations in Affinities of Antibodies during the Immune Response*. Biochemistry 1964, 3 (7), 996-1008.
[cited by applicant]
Fishwild et al. High-avidity human IgG kappa monoclonal antibodies from a novel strain of minilocus transgenic mice. (1996) Nature Biotechnology 14: 845-851.
[cited by applicant]
Forns, et al., Induction of protein-like molecular architecture by monoalkyl hydrocarbon chains. Biopolymers 2000, 54, (7), 531-546.
[cited by applicant]
Forsgren, et al., “Protein A” from
[cited by applicant]
Freire et al., Characterisation of ligand binding by calorimetry. In Biophysical Approaches Determining Ligand Binding to Biomolecular Targets, 2011; pp. 275-299.
[cited by applicant]
Gazit, A possible role for π-stacking in the self-assembly of amyloid fibrils. The FASEB Journal 2002, 16, (1), 77-83.
[cited by applicant]
Gong, Y., et al., “Development of the Double Cyclic Peptide Ligand for Antibody Purification and Protein Detection”, Bioconjugate Chem (2016) 27, 1569-1573.
[cited by applicant]
Greenfield, et al., Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 1969, 8, (10), 4108-4116.
[cited by applicant]
Haines-Butterick, et al., Controlling hydrogelation kinetics by peptide design for three-dimensional encapsulation and injectable delivery of cells. Proceedings of the National Academy of Sciences 2007, 104, (19), 7791-…
[cited by applicant]
Han, et al., Bioinspired self-assembled peptide nanofibers with thermostable multivalent alphahelices. Biomacromolecules 2013, 14, (5), 1594-9.
[cited by applicant]
Handlogten et al., Nonchromatographic affinity precipitation method for the purification of bivalently active pharmaceutical antibodies from biological fluids. Analytical chemistry 2013, 85 (10), 5271-5278.
[cited by applicant]
Hartgerink, et al., Self-assembly and mineralization of peptide-amphiphile nanofibers. Science 2001, 294, (5547), 1684-1688.
[cited by applicant]
Hassouneh et al., Elastin-like polypeptides as a purification tag for recombinant proteins. Curr Protoc Protein Sci 2010, Chapter 6, Unit 611.
[cited by applicant]
Henchey, et al., Contemporary strategies for the stabilization of peptides in the α-helical conformation. Current opinion in chemical biology 2008, 12, (6), 692-697.
[cited by applicant]
Hober et al., Protein A chromatography for antibody purification. J Chromatogr B Analyt Technol Biomed Life Sci 2007, 848 (1), 40-7.
[cited by applicant]
Hol, The role of the α-helix dipole in protein function and structure. Progress in biophysics and molecular biology 1985, 45, (3), 149-195.
[cited by applicant]
Hu et al., Spatiotemporal control of the creation and immolation of peptide assemblies. Coordination Chemistry Reviews 2016, 320, 2-17.
[cited by applicant]
Hu, et al., Electrostatic-Driven Lamination and Untwisting of beta-Sheet Assemblies. ACS Nano 2016, 10, (1), 880-8.
[cited by applicant]
Hudson, et al., The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds. FEBS J 2009, 276, (20), 5960-72.
[cited by applicant]
Huse et al., Purification of antibodies by affinity chromatography. Journal of biochemical and biophysical methods 2002, 51 (3), 217-231.
[cited by applicant]
Huttl, C. et al. Self-assembled peptide amphiphiles function as multivalent binder with increased hemagglutinin affinity. BMC Biotechnol. Jun. 18, 2013;13:51.
[cited by applicant]
Jaenicke, A rapid micromethod for the determination of nitrogen and phosphate in biological material., Anal. Biochem., 61.2 (1974): 623-627.
[cited by applicant]
Jones et al., Replacing the complementarity-determining regions in a human antibody with those from a mouse Nature 321:522-525 (1986).
[cited by applicant]
Karcher, S., et al., “Molecular Biology A Project Approach” Academ Press (1995) pp. 79-81.
[cited by applicant]
Kawashima et al., EpCAM- and EGFR-targeted selective gene therapy for biliary cancers using Z33-fiber modified adenovirus. Int J Cancer 2011, 129 (5), 1244-53.
[cited by applicant]
Kenan, D., et al., “Peptide-PEG Amphiphiles as Cytophobic Coatings for Mammalian and Bacterial Cells” Chemistry & Biology 13, 695-700, Jul. 2006 DOI 10.1016/j.chembiol.2006.06.013.
[cited by applicant]
Kickhoefer et al., Targeting vault nanoparticles to specific cell surface receptors. Acs Nano 2008, 3 (1), 27-36.
[cited by applicant]
Kohler et al., Continuous cultures of fused cells secreting antibody of predefined specificity., Nature 256:495 (1975).
[cited by applicant]
Kokkoli, et al., Self-assembly and applications of biomimetic and bioactive peptide-amphiphiles. Soft Matter 2006, 2, (12), 1015.
[cited by applicant]
Korevaar, et al., Pathway selection in peptide amphiphile assembly. J Am Chem Soc 2014, 136, (24), 8540-3.
[cited by applicant]
Koutsopoulos et al., Two-layered injectable self-assembling peptide scaffold hydrogels for long-term sustained release of human antibodies. J Control Release 2012, 160 (3), 451-8.
[cited by applicant]
Leung, et al., Molecular Crystallization Controlled by pH Regulates Mesoscopic Membrane Morphology. ACS Nano 2012, 6, (12), 10901-10909.
[cited by applicant]
Li, Y., et al., “Bioinspired supramolecular engineering of self-assembling immunofibers for high affinity binding of mmunoglobulin G” Biomaterials 178 (2018) 448-457.
[cited by applicant]
Lin, et al., Supramolecular filaments containing a fixed 41% paclitaxel loading. Chem Commun (Camb) 2013, 49, (43), 4968-70.
[cited by applicant]
Lin, et al., Supramolecular Polymers Formed by ABC Miktoarm Star Peptides. ACS Macro Lett 2013, 2, (12), 1088-1094.
[cited by applicant]
Lock et al., Tuning Cellular Uptake of Molecular Probes by Rational Design of Their Assembly into Supramolecular Nanoprobes. Journal of the American Chemical Society 2016, 138 (10), 3533-3540.
[cited by applicant]
Lock, et al., One-Component Supramolecular Filament Hydrogels as Theranostic Label-Free Magnetic Resonance Imaging Agents. ACS Nano 2017, 11, (1), 797-805.
[cited by applicant]
Lock, et al., Self-assembly of natural and synthetic drug amphiphiles into discrete supramolecular nanostructures. Faraday Discussions 2013, 166, 285.
[cited by applicant]
Lockwood, et al., Acylation of SC4 dodecapeptide increases bactericidal potency against Grampositive bacteria, including drug-resistant strains. Biochemical Journal 2004, 378, (1), 93-103.
[cited by applicant]
Low et al., Future of antibody purification. J Chromatogr B Analyt Technol Biomed Life Sci 2007, 848 (1), 48-63.
[cited by applicant]
Lowik, et al., Tuning secondary structure and self-assembly of amphiphilic peptides. Langmuir 2005, 21, (2), 524-526.
[cited by applicant]
Luan et al. Peptide amphiphiles with multifunctional fragments promoting cellular uptake and endosomal escape as efficient gene vectors. Journal of Materials Chemistry B. 2015, vol. 3, pp. 1068-1078. (Year: 2015).
[cited by applicant]
Lund et al., Exploring variation in binding of Protein A and Protein G to immunoglobulin type G by isothermal titration calorimetry. J Mol Recognit 2011, 24 (6), 945-52.
[cited by applicant]
Luo, et al., Structural dynamic of a self-assembling peptide d-EAK16 made of only D-amino acids. PLoS One 2008, 3, (5), e2364.
[cited by applicant]
Ma et al., Building nanostructures with drugs. Nano Today 2016, 11 (1), 13-30.
[cited by applicant]
Madan et al., ELP-z and ELP-zz capturing scaffolds for the purification of immunoglobulins by affinity precipitation. J Biotechnol 2013, 163 (1), 10-6.
[cited by applicant]
Marks et al., By-passing immunization: human antibodies from V-gene libraries displayed on phage J. Mol. Biol. 222:581-597 (1991).
[cited by applicant]
Marqusee, et al., Unusually stable helix formation in short alanine-based peptides. Proceedings of the National Academy of Sciences 1989, 86, (14), 5286-5290.
[cited by applicant]
Meng, et al., Nanostructures from the self-assembly of alpha-helical peptide amphiphiles. J Pept Sci 2014, 20, (3), 223-8.
[cited by applicant]
Moks et al., Staphylococcal protein A consists of five IgG-binding domains. European Journal of Biochemistry 1986, 156 (3), 637-643.
[cited by applicant]
Morrison et al., Chimeric human antibody molecules: mouse antigen-binding domains with human constant region domains Proc. Natl. Acad. Sci. USA 81:6851-6855 (1984).
[cited by applicant]
Moyer et al., pH and Amphiphilic Structure Direct Supramolecular Behavior in Biofunctional Assemblies. Journal of the American Chemical Society 2014, 136 (42), 14746-14752.
[cited by applicant]
Neame, et al., Inexpensive liquid scintillation counting of aqueous samples. Anal Biochem 1974, 57, (2), 623-627.
[cited by applicant]
Nelson, et al., Stabilization of the ribonuclease S-peptide α-helix by trifluoroethanol. Proteins: Structure, Function, and Bioinformatics 1986, 1, (3), 211-217.
[cited by applicant]
Nilsson et al., A synthetic IgG-binding domain based on staphylococcal protein A. Protein engineering 1987, 1 (2), 107-113.
[cited by applicant]
Nowak, et al., Rapidly recovering hydrogel scaffolds from self-assembling diblock copolypeptide amphiphiles. Nature 2002, 417, (6887), 424-428.
[cited by applicant]
Oeding, et al., Immunochemical Studies on Antigen Preparations from
[cited by applicant]
Office Action for CN Application No. 201880068434.1, mailed Nov. 4, 2022, 10 pages.
[cited by applicant]
Office Action for JP 2020-509080, mailed Apr. 4, 2023, 3 pages. With English translation.
[cited by applicant]
Office Action for JP Application No. 2020-509080, mailed Jul. 12, 2022, 10 pages.
[cited by applicant]
Olszewski et al.,Folding simulations and computer redesign of protein A three-helix bundle motifs. Proteins 1996, 25.
[cited by applicant]
Palmer, et al., Molecular self-assembly into one-dimensional nanostructures. Accounts of chemical research 2008, 41, (12), 1674.
[cited by applicant]
Paramonov, et al., Self-assembly of peptide-amphiphile nanofibers: the roles of hydrogen bonding and amphiphilic packing. Journal of the American Chemical Society 2006, 128, (22), 7291-7298.
[cited by applicant]
Pille, J., et al., “General Strategy for Ordered Noncovalent Protein Assembly on Well-Defined Nanoscaffolds” Biomacromolecules 2013, 14, 4351-4359; dx.doi.org/10.1021/bm401291u.
[cited by applicant]
Presta, Antibody engineering., Curr. Op. Struct. Biol. 2:593-596 (1992).
[cited by applicant]
Richmond, et al., Packing of alpha-helices: Geometrical constraints and contact areas. J. Mol. Biol. 1978, 119, (4), 537-555.
[cited by applicant]
Riechmann et al., Reshaping human antibodies for therapy Nature 332:323-329 (1988).
[cited by applicant]
Rudra, et al., Modulating adaptive immune responses to peptide self-assemblies. Acs Nano 2012, 6, (2), 1557.
[cited by applicant]
Sheth et al., Affinity precipitation of a monoclonal antibody from an industrial harvest feedstock using an ELP-Z stimuli responsive biopolymer. Biotechnol Bioeng 2014, 111 (8), 1595-603.
[cited by applicant]
Sheth et al., Development of an ELP-Z based mAb affinity precipitation process using scaled-down filtration techniques. J Biotechnol 2014, 192 Pt A, 11-9.
[cited by applicant]
Shimada et al., Wormlike micelle formation in peptide-lipid conjugates driven by secondary structure transformation of the headgroups. The journal of physical chemistry. B 2009, 113 (42), 13711-4.
[cited by applicant]
Shukla et al., Downstream processing of monoclonal antibodies—application of platform approaches. J Chromatogr B Analyt Technol Biomed Life Sci 2007, 848 (1), 28-39.
[cited by applicant]
Smith, et al., Fmoc-Diphenylalanine Self Assembles to a Hydrogel via a Novel Architecture Based on Π-π Interlocked β-Sheets. Advanced Materials 2008, 20, (1), 37-41.
[cited by applicant]
Sorokina, I.A., et al., “Guidance manual, large laboratory practical course 2” Biochemistry of Proteins and Peptides, Rostov-on-Don, 2010, p. 96.
[cited by applicant]
Starovasnik et al., Structural mimicry of a native protein by a minimized binding domain. Proceedings of the National Academy of Sciences 1997, 94 (19), 10080-10085.
[cited by applicant]
Strable, E., et al., “Unnatural Amino Acid Incorporation into Virus-Like Particles” Bioconjug Chem. Apr. 2008 ; 19(4): 866-875. doi:10.1021/bc700390r.
[cited by applicant]
Stuart, et al., The use of Nile Red to monitor the aggregation behavior in ternary surfactant-water-organic solvent systems. Journal of physical organic chemistry 2005, 18, (9), 929-934.
[cited by applicant]
Takahashi, et al., Optimization of hydrophobic domains in peptides that undergo transformation from α- helix to β-fibril. Bioorganic & medicinal chemistry 1999, 7, (1), 177-185.
[cited by applicant]
Taylor et al. A transgenic mouse that expresses a diversity of human sequence heavy and light chain immunoglobulins (1992) Nucleic Acids Research 20:6287-6295.
[cited by applicant]
Taylor et al., Human immunoglobulin transgenes undergo rearrangement, somatic mutation and class switching in mice that lack endogenous IgM. (1994) International Immunology 6: 579-591.
[cited by applicant]
Trent et a., Structural properties of soluble peptide amphiphile micelles. Soft Matter 2011, 7 (20), 9572-9582.
[cited by applicant]
Trent, et al., Peptide amphiphile micelles self-adjuvant group A streptococcal vaccination. AAPS J 2015, 17, (2), 380-8.
[cited by applicant]
Tuaillon et al. Human immunoglobulin heavy-chain minilocus recombination in transgenic mice: gene-segment use in mu and gamma transcripts.(1993) Proc. Natl. Acad. Sci. USA 90:3720-3724.
[cited by applicant]
Tuaillon et al., Biased utilization of DHQ52 and JH4 gene segments in a human Ig transgenic minilocus is independent of antigenic selection. (1994) J. Immunol. 152:2912-2920.
[cited by applicant]
Ulijn, et al., Designing peptide based nanomaterials. Chem Soc Rev 2008, 37, (4), 664-75.
[cited by applicant]
Vaneldijk, M. , et al., “Thermodynamic investigation of Z33-antibody interaction leads to selective purification of human antibodies” Joumal of Biotechnology 179 (2014) 32-41.
[cited by applicant]
Vauthey, et al., Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles. Proceedings of the National Academy of Sciences 2002, 99, (8), 5355-5360.
[cited by applicant]
Webber et al., Reprint of: Development of bioactive peptide amphiphiles for therapeutic cell delivery. Acta biomaterialia 2015, 23, S42-S51.
[cited by applicant]
Webber, et al., Development of bioactive peptide amphiphiles for therapeutic cell delivery. Acta Biomater 2010, 6, (1), 3-11.
[cited by applicant]
Wiseman et al., Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Analytical biochemistry 1989, 179 (1), 131-137.
[cited by applicant]
Xu, et al., Hydrophobic-region-induced transitions in self-assembled peptide nanostructures. Langmuir 2008, 25, (7), 4115-4123.
[cited by applicant]
Zhao, et al., Molecular hydrogels of therapeutic agents. Chem Soc Rev 2009, 38, (4), 883-91.
[cited by applicant]
Missirlis, D. et al. Mechanisms of peptide amphiphile internalization by SJSA-1 cells in vitro. Biochemistry. Apr. 21, 2009;48(15):3304-14.
[cited by applicant]
Office Action for KR 10-2020-7007663, mailed Feb. 26, 2024, 9 pages. With English Translation.
[cited by applicant]
Cited By (1)