IP Library Granted Patent US 12,410,213
Granted Patent B2
US 12,410,213 · App. 17/265,765 · Granted Sep 9, 2025

Polypeptides self-assembling into nanoparticles

Inventors: Thomas George Watt Edwardson (Zürich, CH); Donald Hilvert (Zürich, CH)
Assignee: ETH ZËRICH
C07K14/001C12N15/113C12N15/88C07K2319/21C12N2310/14C12N2310/3513
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 12,410,213
App. No.
17/265,765
Granted
Sep 9, 2025
Kind
B2
Abstract

The present invention relates to polypeptides self-assembling into nanoparticles. In particular, the invention relates to a polypeptide comprising an amino acid sequence I (SEQ ID NO: 1), a nucleic acid sequence encoding said polypeptide, a nanoparticle comprising at least one polypeptide of the invention, a complex comprising said nanoparticle and one or more cargo molecules, and a method for transfecting a cell with said complex.

Claims (20)

1. A polypeptide comprising an amino acid sequence I, wherein said amino acid sequence I is an amino acid sequence selected from the group consisting of SEQ ID NO: 2 to 5 and SEQ ID NO: 10 to 16, 37 and 38.

2. The polypeptide of claim 1 , wherein said amino acid sequence I is an amino acid sequence selected from the group consisting of SEQ ID NO: 2 to 5 and SEQ ID NO: 10 to 16.

3. The polypeptide of claim 1 , wherein said polypeptide further comprises a histidine tag, wherein said histidine tag consists of at least two consecutively linked histidines (His tag).

4. The polypeptide of claim 3 , wherein said His tag consists of 6 consecutively linked histidines (His6 tag).

5. The polypeptide of claim 1 , wherein said amino acid sequence I is the amino acid sequence of SEQ ID NO: 2.

6. The polypeptide of claim 1 , wherein said amino acid sequence I is the amino acid sequence of SEQ ID NO: 4.

7. The polypeptide of claim 1 , wherein said amino acid sequence I is the amino acid sequence of SEQ ID NO: 5.

8. The polypeptide of claim 1 , wherein said amino acid sequence I is the amino acid sequence of SEQ ID NO: 10.

9. The polypeptide of claim 1 , wherein said amino acid sequence I is the amino acid sequence of SEQ ID NO: 12.

10. The polypeptide of claim 1 , wherein said amino acid sequence I is the amino acid sequence of SEQ ID NO: 13.

11. The polypeptide of claim 1 , wherein said amino acid sequence I is the amino acid sequence of SEQ ID NO: 14.

12. The polypeptide of claim 1 , wherein said amino acid sequence I is the amino acid sequence of SEQ ID NO: 15.

13. The polypeptide of claim 1 , wherein said amino acid sequence I is the amino acid sequence of SEQ ID NO: 16.

14. A nucleic acid sequence encoding the polypeptide of claim 1 .

15. A nanoparticle comprising at least one polypeptide according to claim 1 .

16. A complex comprising the nanoparticle of claim 15 and one or more cargo molecules, wherein said one or more cargo molecules are encapsulated in said nanoparticle.

17. The complex of claim 16 , wherein said one or more cargo molecules are one or more oligonucleotides.

18. The complex of claim 17 , wherein said one or more oligonucleotides encapsulated in said nanoparticle are not accessible to DNAse hydrolysis.

19. The complex of claim 17 , wherein said one or more oligonucleotides are RNA selected from the group consisting of antisense oligonucleotides (ASO), small interference RNA (siRNA), small hairpin RNA (shRNA), micro RNA (miRNA) and anti-miRNA.

20. A method for transfecting a cell comprising the step of contacting said cell with the complex of claim 16 .

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Feb 3, 2021
From: EDWARDSON, THOMAS GEORGE WATT; HILVERT, DONALD
To: ETH ZURICH
Reel/Frame 055136/0474 →
Priority Claims (1)
EP 18187862 · Aug 7, 2018 · regional
Continuity (1)
Related Publication 20210163540A1 · Jun 3, 2021
References Cited (26)
US 20130274441A1 · Baker · 2013 [cited by examiner]
US 20160122392A1 · Baker et al. · 2016 [cited by applicant]
US 20180318218A1 · Kamrud et al. · 2018 [cited by applicant]
US 20230080270A1 · Hilvert · 2023 [cited by examiner]
CN 103694317A · 2014 [cited by applicant]
WO 2010035009A1 · 2010 [cited by applicant]
WO WO2015054639A1 · 2015 [cited by examiner]
WO 2016138525A1 · 2016 [cited by applicant]
Lilavivat, S., Sardar, D., Jana, S., Thomas, G. C., & Woycechowsky, K. J. In vivo encapsulation of nucleic acids using an engineered nonviral protein capsid. Journal of the American Chemical Society, 134(32), 13152-1315… [cited by examiner]
Azuma, Y., Edwardson, T. G., & Hilvert, D. Tailoring lumazine synthase assemblies for bionanotechnology. Chemical Society Reviews, 47(10), 3543-3557. (Year: 2018). [cited by examiner]
Azuma et al., “Tailoring Lumazine Synthase Assemblies for Bionanotechnology,” Chemical Society Reviews 47 (10):3543-3557 (2018). [cited by applicant]
Cai et al., “Polypeptide Self-Assemblies: Nanostructures and Bioapplications,” Chemical Society Reviews 45 (21): 5985-6012 (2016). [cited by applicant]
Edwardson et al., “Rational Engineering of a Designed Protein Cage for siRNA Delivery,” Journal of the American Chemical Society 140(33):10439-10442 (2018). [cited by applicant]
King et al., “Computational Design of Self-Assembling Protein Nanomaterials with Atomic Level Accuracy,” Science 336(6085):1171-1174 (2012). [cited by applicant]
Lilavivat et al., “In Vivo Encapsulation of Nucleic Acids Using an Engineered Nonviral Protein Capsid,” Journal of the American Chemical Society 134(32):13152-13155 (2012). [cited by applicant]
International Search Report issued in Int'l Appl. No. PCT/EP2019/071143, mailed Sep. 23, 2019. [cited by applicant]
Heinze et al., “Protein Nanocontainers from Nonviral Origin: Testing the Mechanics of Artificial and Natural Protein Cages by AFM”, The Journal of Physical Chemistry B 120(26):5945-5952 (2016). [cited by applicant]
Bayburt et al., “Self-Assembly of Discoidal Phospholipid Bilayer Nanoparticles with Membrane Scaffold Proteins,” Nano Letters 2(8):853-85 (2002). [cited by applicant]
Chang et al., “Curvature Dependence of Viral Protein Structures on Encapsidated Nanoemulsion Droplets,” ACS Nano 2:281-286 (2008). [cited by applicant]
Chidchob, et al., “Synergy of Two Assembly Languages in DNA Nanostructures: Self-Assembly of Sequence-Defined Polymers on DNA Cages,” J. Am. Chem. Soc. 138:4416-4425 (2016). [cited by applicant]
Edwardson et al., “Site-specific positioning of dendritic alkyl chains on DNA cages enables their geometry-dependent self-assembly,” Nature Chemistry 5:868 (2013). [cited by applicant]
Kwak et al., “Virus-like Particles Templated by DNA Micelles: A General Method for Loading Virus Nanocarriers,” J. Am. Chem. Soc. 132:7834-7835 (2010). [cited by applicant]
Loredo-Tovias et al., “Encapsidated ultrasmall nanolipospheres as novel nanocarriers for highly hydrophobic anticancer drugs,” Nanoscale 9:11625-11631 (2017). [cited by applicant]
Olzmann and Carvalho, “Dynamics and functions of lipid droplets,” Nat. Rev. Mol. Cell Biol. 20:137-155 (2019). [cited by applicant]
Ordovas, J. M. in Encyclopedia of Food Sciences and Nutrition (Second Edition) (ed Benjamin Caballero) 3543-3552 Academic Press (2003). [cited by applicant]
Spicer et al., “Peptide and protein nanoparticle conjugates: versatile platforms for biomedical applications,” Chem. Soc. Rev. 47:3574-3620 (2018). [cited by applicant]