Antiviral fibrils of self-assembled peptides with tunable compositions

Joseph Dodd-o, Abhishek Roy, Zain Siddiqui, Roya Jafari, Francesco Coppola, Santhamani Ramasamy, Afsal Kolloli, Dilip Kumar, Soni Kaundal, Boyang Zhao, Ranjeet Kumar, Alicia S. Robang, Jeffrey Li, Abdul-Rahman Azizogli, Varun Pai, Amanda Acevedo-Jake, Corey Heffernan, Alexandra Lucas, Andrew C. McShan, Anant K. Paravastu, B. V. Venkataram Prasad, Selvakumar Subbian, Petr Král () and Vivek Kumar ()
Additional contact information
Joseph Dodd-o: New Jersey Institute of Technology
Zain Siddiqui: New Jersey Institute of Technology
Roya Jafari: University of Illinois at Chicago
Francesco Coppola: University of Illinois at Chicago
Santhamani Ramasamy: Rutgers University
Afsal Kolloli: Rutgers University
Dilip Kumar: Baylor College of Medicine
Soni Kaundal: Baylor College of Medicine
Boyang Zhao: Baylor College of Medicine
Ranjeet Kumar: Rutgers University
Alicia S. Robang: Georgia Institute of Technology
Jeffrey Li: Georgia Institute of Technology
Abdul-Rahman Azizogli: New Jersey Institute of Technology
Varun Pai: New Jersey Institute of Technology
Amanda Acevedo-Jake: New Jersey Institute of Technology
Corey Heffernan: New Jersey Institute of Technology
Alexandra Lucas: Biodesign Institute, Arizona State University
Andrew C. McShan: Georgia Institute of Technology
Anant K. Paravastu: Georgia Institute of Technology
B. V. Venkataram Prasad: Baylor College of Medicine
Selvakumar Subbian: Rutgers University
Petr Král: University of Illinois at Chicago
Vivek Kumar: New Jersey Institute of Technology

Nature Communications, 2024, vol. 15, issue 1, 1-14

Abstract: 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.

Date: 2024
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DOI: 10.1038/s41467-024-45193-3

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