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COVID-19: insights into virus–receptor interactions
The recent outbreak of Coronavirus Disease 2019 (COVID-19) calls for rapid mobilization of scientists to probe and explore solutions to this deadly disease. A limited understanding of the high transmissibility of SARS-CoV-2 (Severe acute respiratory syndrome coronavirus 2) relative to other coronavi...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Singapore
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8035060/ https://www.ncbi.nlm.nih.gov/pubmed/34766003 http://dx.doi.org/10.1186/s43556-021-00033-4 |
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author | Sepahvandi, Azadeh Ghaffari, Maryam Bahmanpour, Amir Hossein Moztarzadeh, Fathollah Zarrintaj, Payam Uludağ, Hasan Mozafari, Masoud |
author_facet | Sepahvandi, Azadeh Ghaffari, Maryam Bahmanpour, Amir Hossein Moztarzadeh, Fathollah Zarrintaj, Payam Uludağ, Hasan Mozafari, Masoud |
author_sort | Sepahvandi, Azadeh |
collection | PubMed |
description | The recent outbreak of Coronavirus Disease 2019 (COVID-19) calls for rapid mobilization of scientists to probe and explore solutions to this deadly disease. A limited understanding of the high transmissibility of SARS-CoV-2 (Severe acute respiratory syndrome coronavirus 2) relative to other coronavirus strains guides a deeper investigation into the virus/receptor interactions. The cutting-edge studies in thermodynamic and kinetic properties of interactions such as protein-protein interplays have been reviewed in many modeling and analysis studies. Highlighting the thermodynamic assessments of biological interactions and emphasizing the boosted transmissibility of SARS-CoV-2 despite its high similarity in structure and sequence with other coronavirus strains is an important and highly valuable investigation that can lead scientists to discover analytical and fundamental approaches in studying virus’s interactions. Accordingly, we have attempted to describe the crucial factors such as conformational changes and hydrophobicity particularities that influence on thermodynamic potentials in the SARS-COV-2 S-protein adsorption process. Discussing the thermodynamic potentials and the kinetics of the SARS-CoV-2 S-protein in its interaction with the ACE2 receptors of the host cell is a fundamental approach that would be extremely valuable in designing candidate pharmaceutical agents or exploring alternative treatments. |
format | Online Article Text |
id | pubmed-8035060 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Springer Singapore |
record_format | MEDLINE/PubMed |
spelling | pubmed-80350602021-04-12 COVID-19: insights into virus–receptor interactions Sepahvandi, Azadeh Ghaffari, Maryam Bahmanpour, Amir Hossein Moztarzadeh, Fathollah Zarrintaj, Payam Uludağ, Hasan Mozafari, Masoud Mol Biomed Perspective The recent outbreak of Coronavirus Disease 2019 (COVID-19) calls for rapid mobilization of scientists to probe and explore solutions to this deadly disease. A limited understanding of the high transmissibility of SARS-CoV-2 (Severe acute respiratory syndrome coronavirus 2) relative to other coronavirus strains guides a deeper investigation into the virus/receptor interactions. The cutting-edge studies in thermodynamic and kinetic properties of interactions such as protein-protein interplays have been reviewed in many modeling and analysis studies. Highlighting the thermodynamic assessments of biological interactions and emphasizing the boosted transmissibility of SARS-CoV-2 despite its high similarity in structure and sequence with other coronavirus strains is an important and highly valuable investigation that can lead scientists to discover analytical and fundamental approaches in studying virus’s interactions. Accordingly, we have attempted to describe the crucial factors such as conformational changes and hydrophobicity particularities that influence on thermodynamic potentials in the SARS-COV-2 S-protein adsorption process. Discussing the thermodynamic potentials and the kinetics of the SARS-CoV-2 S-protein in its interaction with the ACE2 receptors of the host cell is a fundamental approach that would be extremely valuable in designing candidate pharmaceutical agents or exploring alternative treatments. Springer Singapore 2021-04-10 /pmc/articles/PMC8035060/ /pubmed/34766003 http://dx.doi.org/10.1186/s43556-021-00033-4 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Perspective Sepahvandi, Azadeh Ghaffari, Maryam Bahmanpour, Amir Hossein Moztarzadeh, Fathollah Zarrintaj, Payam Uludağ, Hasan Mozafari, Masoud COVID-19: insights into virus–receptor interactions |
title | COVID-19: insights into virus–receptor interactions |
title_full | COVID-19: insights into virus–receptor interactions |
title_fullStr | COVID-19: insights into virus–receptor interactions |
title_full_unstemmed | COVID-19: insights into virus–receptor interactions |
title_short | COVID-19: insights into virus–receptor interactions |
title_sort | covid-19: insights into virus–receptor interactions |
topic | Perspective |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8035060/ https://www.ncbi.nlm.nih.gov/pubmed/34766003 http://dx.doi.org/10.1186/s43556-021-00033-4 |
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