journal article·2026-07-26

Self-Assembly of Virus-like Nanoparticles for Nucleic Acid Delivery Based on De Novo Designed α-Helix Peptides

Mingshan Han, Jintao Feng, Xi Rong, Yuzhi Ye, Xinhao Jiao, Lei Shang, Wenbin Zhang, Yue Zhao, Wei Qi, Rongxin Su, Yuefei Wang

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Abstract

Efficient and safe delivery of nucleic acids remains a major challenge for clinical translation of gene therapies. Here, we report de novo-designed α-helical peptides that coassemble with lipids and nucleic acids to form core-shell, virus-like nanoparticles (VLNs). The peptides combine a cationic N-terminus for nucleic acid binding, an anionic C-terminus for lipid coordination, and pH-responsive residues that promote endolysosomal escape. The resulting VLNs achieved up to 91.2% mRNA transfection and 93.1% siRNA-mediated gene knockdown in vitro, outperforming Lipofectamine 2000. This work demonstrates a programmable, rational design strategy to produce virus-mimetic nanocarriers that address key extracellular and intracellular barriers in nucleic acid therapeutics.
Source: europepmc · Quality: candidate unverified · Source record ↗

Research context

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

School of Chemical Engineering and Technology, State Key Laboratory of Chemical Engineering and Low-Carbon Technology

Tianjin University

Network Center of Tianjin University

Collaborative Innovation Center of Chemical Science and Engineering (Tianjin)

Tianjin Key Laboratory of Membrane Science and Desalination Technology

Funding

Tianjin Municipal Science and Technology Bureau · National Natural Science Foundation of China

References (32)

Show source-provided references
1. 10.1126/science.aan467210.1126/science.aan4672 ↗
2. 10.1016/j.cell.2022.03.04510.1016/j.cell.2022.03.045 ↗
3. 10.1007/s41061-017-0115-x10.1007/s41061-017-0115-x ↗
4. 10.1002/advs.20200370610.1002/advs.202003706 ↗
5. 10.1016/j.addr.2021.11399810.1016/j.addr.2021.113998 ↗
6. 10.1016/j.jconrel.2020.09.00310.1016/j.jconrel.2020.09.003 ↗
7. 10.1021/jacs.5c0303310.1021/jacs.5c03033 ↗
8. 10.1039/D4CB00295D10.1039/D4CB00295D ↗
9. 10.1073/pnas.171296311510.1073/pnas.1712963115 ↗
10. 10.1002/adma.20110231310.1002/adma.201102313 ↗
11. 10.1021/acsanm.2c0427910.1021/acsanm.2c04279 ↗
12. 10.1002/smll.20220495910.1002/smll.202204959 ↗
13. 10.1002/ange.20180586810.1002/ange.201805868 ↗
14. 10.1038/s41557-021-00854-410.1038/s41557-021-00854-4 ↗
15. 10.1021/acsnano.3c0266910.1021/acsnano.3c02669 ↗
16. 10.1038/s41578-025-00814-110.1038/s41578-025-00814-1 ↗
17. 10.1093/bioinformatics/btq00710.1093/bioinformatics/btq007 ↗
18. Leaver-Fay A. · 2011 · 487 · 545
19. 10.1126/science.add218710.1126/science.add2187 ↗
20. 10.1038/s41586-021-03819-210.1038/s41586-021-03819-2 ↗
21. 10.1126/science.abc818210.1126/science.abc8182 ↗
22. 10.1126/science.125748110.1126/science.1257481 ↗
23. 10.1038/nature1801010.1038/nature18010 ↗
24. 10.1126/science.aaf881810.1126/science.aaf8818 ↗
25. 10.1021/jacs.8b0644210.1021/jacs.8b06442 ↗
26. 10.1002/9780470015902.a0001091.pub210.1002/9780470015902.a0001091.pub2 ↗
27. 10.1021/acsnano.5c1287110.1021/acsnano.5c12871 ↗
28. 10.1107/S0365110X5300195210.1107/S0365110X53001952 ↗
29. 10.1038/nprot.2006.20210.1038/nprot.2006.202 ↗
30. 10.1126/science.aav789710.1126/science.aav7897 ↗
31. 10.1002/smll.20120112910.1002/smll.201201129 ↗
32. 10.1021/acs.bioconjchem.3c0010410.1021/acs.bioconjchem.3c00104 ↗