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Antiviral fibrils of self-assembled peptides with tunable compositions.
Dodd-O, Joseph; Roy, Abhishek; Siddiqui, Zain; Jafari, Roya; Coppola, Francesco; Ramasamy, Santhamani; Kolloli, Afsal; Kumar, Dilip; Kaundal, Soni; Zhao, Boyang; Kumar, Ranjeet; Robang, Alicia S; Li, Jeffrey; Azizogli, Abdul-Rahman; Pai, Varun; Acevedo-Jake, Amanda; Heffernan, Corey; Lucas, Alexandra; McShan, Andrew C; Paravastu, Anant K; Prasad, B V Venkataram; Subbian, Selvakumar; Král, Petr; Kumar, Vivek.
Affiliation
  • Dodd-O J; Department of Biomedical Engineering, New Jersey Institute of Technology, Newark, NJ, 07102, USA.
  • Roy A; Department of Biomedical Engineering, New Jersey Institute of Technology, Newark, NJ, 07102, USA.
  • Siddiqui Z; Department of Biomedical Engineering, New Jersey Institute of Technology, Newark, NJ, 07102, USA.
  • Jafari R; Department of Chemistry, University of Illinois at Chicago, Chicago, IL, 60607, USA.
  • Coppola F; Department of Chemistry, University of Illinois at Chicago, Chicago, IL, 60607, USA.
  • Ramasamy S; Public Health Research Institute, New Jersey Medical School, Rutgers University, Newark, NJ, 07103, USA.
  • Kolloli A; Public Health Research Institute, New Jersey Medical School, Rutgers University, Newark, NJ, 07103, USA.
  • Kumar D; Department of Molecular Virology & Microbiology, Baylor College of Medicine, Houston, TX, 77030, USA.
  • Kaundal S; Department of Molecular Virology & Microbiology, Baylor College of Medicine, Houston, TX, 77030, USA.
  • Zhao B; Department of Molecular Virology & Microbiology, Baylor College of Medicine, Houston, TX, 77030, USA.
  • Kumar R; Public Health Research Institute, New Jersey Medical School, Rutgers University, Newark, NJ, 07103, USA.
  • Robang AS; School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA, 30332, USA.
  • Li J; School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA, 30332, USA.
  • Azizogli AR; Department of Biological Sciences, New Jersey Institute of Technology, Newark, NJ, 07102, USA.
  • Pai V; Department of Biological Sciences, New Jersey Institute of Technology, Newark, NJ, 07102, USA.
  • Acevedo-Jake A; Department of Biomedical Engineering, New Jersey Institute of Technology, Newark, NJ, 07102, USA.
  • Heffernan C; Department of Biomedical Engineering, New Jersey Institute of Technology, Newark, NJ, 07102, USA.
  • Lucas A; SAPHTx Inc, Newark, NJ, 07104, USA.
  • McShan AC; Center for Personalized Diagnostics and Center for Immunotherapy Vaccines and Virotherapy, Biodesign Institute, Arizona State University, 727 E, Tempe, AZ, USA.
  • Paravastu AK; School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA, 30332, USA.
  • Prasad BVV; School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA, 30332, USA.
  • Subbian S; Department of Molecular Virology & Microbiology, Baylor College of Medicine, Houston, TX, 77030, USA.
  • Král P; Public Health Research Institute, New Jersey Medical School, Rutgers University, Newark, NJ, 07103, USA.
  • Kumar V; Department of Chemistry, University of Illinois at Chicago, Chicago, IL, 60607, USA. pkral@uic.edu.
Nat Commun ; 15(1): 1142, 2024 Feb 07.
Article in En | MEDLINE | ID: mdl-38326301
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 ß-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.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: COVID-19 Limits: Humans Language: En Journal: Nat Commun Journal subject: BIOLOGIA / CIENCIA Year: 2024 Document type: Article Affiliation country:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: COVID-19 Limits: Humans Language: En Journal: Nat Commun Journal subject: BIOLOGIA / CIENCIA Year: 2024 Document type: Article Affiliation country: