Antiviral fibrils of self-assembled peptides with tunable compositions
Document Type
Article
Publication Date
12-1-2024
Abstract
The lasting threat of viral pandemics necessitates the development of tailorable first-response antivirals with specific but adaptive architectures for treatment of novel viral infections. Here, such an antiviral platform has been developed based on a mixture of hetero-peptides self-assembled into functionalized β-sheets capable of specific multivalent binding to viral protein complexes. One domain of each hetero-peptide is designed to specifically bind to certain viral proteins, while another domain self-assembles into fibrils with epitope binding characteristics determined by the types of peptides and their molar fractions. The self-assembled fibrils maintain enhanced binding to viral protein complexes and retain high resilience to viral mutations. This method is experimentally and computationally tested using short peptides that specifically bind to Spike proteins of SARS-CoV-2. This platform is efficacious, inexpensive, and stable with excellent tolerability.
Identifier
85184698292 (Scopus)
Publication Title
Nature Communications
External Full Text Location
https://doi.org/10.1038/s41467-024-45193-3
e-ISSN
20411723
PubMed ID
38326301
Issue
1
Volume
15
Grant
R21AR079708
Fund Ref
National Institutes of Health
Recommended Citation
Dodd-o, Joseph; Roy, Abhishek; Siddiqui, Zain; Jafari, Roya; Coppola, Francesco; Ramasamy, Santhamani; Kolloli, Afsal; Kumar, Dilip; Kaundal, Soni; Zhao, Boyan; Kumar, Ranjeet; Robang, Alicia S.; Li, Jeffrey; Azizogli, Abdul Rahman; Pai, Varun; Acevedo-Jake, Amanda; Heffernan, Corey; Lucas, Alexandra; McShan, Andrew C.; and Paravastu, Anant K., "Antiviral fibrils of self-assembled peptides with tunable compositions" (2024). Faculty Publications. 77.
https://digitalcommons.njit.edu/fac_pubs/77
