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Phage Display-Derived Peptide for the Specific Binding of SARS-CoV-2
[Image: see text] Beginning from the end of 2019, the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic swept all over the world and is still afflicting the whole global population. Given that the vaccine-manufacturing ability is limited and the virus can evolve quickly, vaccinat...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8751651/ https://www.ncbi.nlm.nih.gov/pubmed/35128233 http://dx.doi.org/10.1021/acsomega.1c04873 |
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author | Yang, Fan Liu, Li Neuenschwander, Pierre Fernand Idell, Steven Vankayalapati, Ramakrishna Jain, Krishan Gopal Du, Ke Ji, Honglong Yi, Guohua |
author_facet | Yang, Fan Liu, Li Neuenschwander, Pierre Fernand Idell, Steven Vankayalapati, Ramakrishna Jain, Krishan Gopal Du, Ke Ji, Honglong Yi, Guohua |
author_sort | Yang, Fan |
collection | PubMed |
description | [Image: see text] Beginning from the end of 2019, the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic swept all over the world and is still afflicting the whole global population. Given that the vaccine-manufacturing ability is limited and the virus can evolve quickly, vaccination alone may not be able to end the pandemic, thus developing fast and accurate diagnoses and effective therapeutics will always be unmet needs. Phage display peptide library has been used in screening antigen-specific peptides for the invention of novel mimic receptors/ligands. Here, we report that a 12-mer phage display peptide library has been screened against the SARS-CoV-2 receptor-binding domain (RBD), and five of the screened peptides show binding ability with the RBD protein by the enzyme-linked immune sorbent assay. The surface plasmon resonance assay further demonstrates that peptide no. 1 can specifically bind to SARS-CoV-2 RBD with a binding affinity constant (K(d)) of 5.8 μM. Transmission electron microscopy coupled with a magnetic bead assay further confirms that the screened peptide can specifically bind the inactivated SARS-CoV-2 virus. This SARS-CoV-2-specific peptide holds great promise as a new bioreceptor/ligand for the rapid and accurate detection of SARS-CoV-2. |
format | Online Article Text |
id | pubmed-8751651 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-87516512022-01-11 Phage Display-Derived Peptide for the Specific Binding of SARS-CoV-2 Yang, Fan Liu, Li Neuenschwander, Pierre Fernand Idell, Steven Vankayalapati, Ramakrishna Jain, Krishan Gopal Du, Ke Ji, Honglong Yi, Guohua ACS Omega [Image: see text] Beginning from the end of 2019, the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic swept all over the world and is still afflicting the whole global population. Given that the vaccine-manufacturing ability is limited and the virus can evolve quickly, vaccination alone may not be able to end the pandemic, thus developing fast and accurate diagnoses and effective therapeutics will always be unmet needs. Phage display peptide library has been used in screening antigen-specific peptides for the invention of novel mimic receptors/ligands. Here, we report that a 12-mer phage display peptide library has been screened against the SARS-CoV-2 receptor-binding domain (RBD), and five of the screened peptides show binding ability with the RBD protein by the enzyme-linked immune sorbent assay. The surface plasmon resonance assay further demonstrates that peptide no. 1 can specifically bind to SARS-CoV-2 RBD with a binding affinity constant (K(d)) of 5.8 μM. Transmission electron microscopy coupled with a magnetic bead assay further confirms that the screened peptide can specifically bind the inactivated SARS-CoV-2 virus. This SARS-CoV-2-specific peptide holds great promise as a new bioreceptor/ligand for the rapid and accurate detection of SARS-CoV-2. American Chemical Society 2021-12-29 /pmc/articles/PMC8751651/ /pubmed/35128233 http://dx.doi.org/10.1021/acsomega.1c04873 Text en © 2021 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Yang, Fan Liu, Li Neuenschwander, Pierre Fernand Idell, Steven Vankayalapati, Ramakrishna Jain, Krishan Gopal Du, Ke Ji, Honglong Yi, Guohua Phage Display-Derived Peptide for the Specific Binding of SARS-CoV-2 |
title | Phage Display-Derived Peptide for the Specific Binding
of SARS-CoV-2 |
title_full | Phage Display-Derived Peptide for the Specific Binding
of SARS-CoV-2 |
title_fullStr | Phage Display-Derived Peptide for the Specific Binding
of SARS-CoV-2 |
title_full_unstemmed | Phage Display-Derived Peptide for the Specific Binding
of SARS-CoV-2 |
title_short | Phage Display-Derived Peptide for the Specific Binding
of SARS-CoV-2 |
title_sort | phage display-derived peptide for the specific binding
of sars-cov-2 |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8751651/ https://www.ncbi.nlm.nih.gov/pubmed/35128233 http://dx.doi.org/10.1021/acsomega.1c04873 |
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