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Antiviral fibrils of self-assembled peptides with tunable compositions

Author

Listed:
  • Joseph Dodd-o

    (New Jersey Institute of Technology)

  • Abhishek Roy

    (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
    SAPHTx Inc)

  • 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
    University of Illinois at Chicago
    University of Illinois at Chicago
    University of Illinois at Chicago)

  • Vivek Kumar

    (New Jersey Institute of Technology
    New Jersey Institute of Technology
    SAPHTx Inc
    New Jersey Institute of Technology)

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.

Suggested Citation

  • 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 & Jef, 2024. "Antiviral fibrils of self-assembled peptides with tunable compositions," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
  • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-45193-3
    DOI: 10.1038/s41467-024-45193-3
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    References listed on IDEAS

    as
    1. Jun Lan & Jiwan Ge & Jinfang Yu & Sisi Shan & Huan Zhou & Shilong Fan & Qi Zhang & Xuanling Shi & Qisheng Wang & Linqi Zhang & Xinquan Wang, 2020. "Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor," Nature, Nature, vol. 581(7807), pages 215-220, May.
    2. Zhennan Zhao & Jingya Zhou & Mingxiong Tian & Min Huang & Sheng Liu & Yufeng Xie & Pu Han & Chongzhi Bai & Pengcheng Han & Anqi Zheng & Lutang Fu & Yuanzhu Gao & Qi Peng & Ying Li & Yan Chai & Zengyua, 2022. "Omicron SARS-CoV-2 mutations stabilize spike up-RBD conformation and lead to a non-RBM-binding monoclonal antibody escape," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
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