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; Boyan 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; Vivek Kumar

doi:10.1038/s41467-024-45193-3

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, Boyan 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. ParavastuB. V.Venkataram Prasad, Selvakumar Subbian, Petr Král, Vivek Kumar

Bio-Medical Engineering

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

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.

Original language	English (US)
Article number	1142
Journal	Nature communications
Volume	15
Issue number	1
DOIs	https://doi.org/10.1038/s41467-024-45193-3
State	Published - Dec 2024

All Science Journal Classification (ASJC) codes

General Chemistry
General Biochemistry, Genetics and Molecular Biology
General Physics and Astronomy

Access to Document

10.1038/s41467-024-45193-3

Cite this

Dodd-o, J., Roy, A., Siddiqui, Z., Jafari, R., Coppola, F., Ramasamy, S., Kolloli, A., Kumar, D., Kaundal, S., Zhao, B., Kumar, R., Robang, A. S., Li, J., Azizogli, A. R., Pai, V., Acevedo-Jake, A., Heffernan, C., Lucas, A., McShan, A. C., ... Kumar, V. (2024). Antiviral fibrils of self-assembled peptides with tunable compositions. Nature communications, 15(1), Article 1142. https://doi.org/10.1038/s41467-024-45193-3

@article{b4733686074c4bf0b6688d7ef7addf23,

title = "Antiviral fibrils of self-assembled peptides with tunable compositions",

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.",

author = "Joseph Dodd-o and Abhishek Roy and Zain Siddiqui and Roya Jafari and Francesco Coppola and Santhamani Ramasamy and Afsal Kolloli and Dilip Kumar and Soni Kaundal and Boyan Zhao and Ranjeet Kumar and Robang, {Alicia S.} and Jeffrey Li and Azizogli, {Abdul Rahman} and Varun Pai and Amanda Acevedo-Jake and Corey Heffernan and Alexandra Lucas and McShan, {Andrew C.} and Paravastu, {Anant K.} and Prasad, {B. V.Venkataram} and Selvakumar Subbian and Petr Kr{\'a}l and Vivek Kumar",

note = "Publisher Copyright: {\textcopyright} The Author(s) 2024.",

year = "2024",

month = dec,

doi = "10.1038/s41467-024-45193-3",

language = "English (US)",

volume = "15",

journal = "Nature communications",

issn = "2041-1723",

publisher = "Nature Publishing Group",

number = "1",

}

Dodd-o, J, Roy, A, Siddiqui, Z, Jafari, R, Coppola, F, Ramasamy, S, Kolloli, A, Kumar, D, Kaundal, S, Zhao, B, Kumar, R, Robang, AS, Li, J, Azizogli, AR, Pai, V, Acevedo-Jake, A, Heffernan, C, Lucas, A, McShan, AC, Paravastu, AK, Prasad, BVV, Subbian, S, Král, P & Kumar, V 2024, 'Antiviral fibrils of self-assembled peptides with tunable compositions', Nature communications, vol. 15, no. 1, 1142. https://doi.org/10.1038/s41467-024-45193-3

TY - JOUR

T1 - Antiviral fibrils of self-assembled peptides with tunable compositions

AU - Dodd-o, Joseph

AU - Roy, Abhishek

AU - Siddiqui, Zain

AU - Jafari, Roya

AU - Coppola, Francesco

AU - Ramasamy, Santhamani

AU - Kolloli, Afsal

AU - Kumar, Dilip

AU - Kaundal, Soni

AU - Zhao, Boyan

AU - Kumar, Ranjeet

AU - Robang, Alicia S.

AU - Li, Jeffrey

AU - Azizogli, Abdul Rahman

AU - Pai, Varun

AU - Acevedo-Jake, Amanda

AU - Heffernan, Corey

AU - Lucas, Alexandra

AU - McShan, Andrew C.

AU - Paravastu, Anant K.

AU - Prasad, B. V.Venkataram

AU - Subbian, Selvakumar

AU - Král, Petr

AU - Kumar, Vivek

PY - 2024/12

Y1 - 2024/12

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85184698292&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85184698292&partnerID=8YFLogxK

U2 - 10.1038/s41467-024-45193-3

DO - 10.1038/s41467-024-45193-3

M3 - Article

C2 - 38326301

AN - SCOPUS:85184698292

SN - 2041-1723

VL - 15

JO - Nature communications

JF - Nature communications

IS - 1

M1 - 1142

ER -

Antiviral fibrils of self-assembled peptides with tunable compositions

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this