Human Amylin in the Presence of SARS-COV-2 Protein Fragments

[Image: see text] COVID-19 can lead to the onset of type-II diabetes, which is associated with the aggregation of islet amyloid polypeptides, also called amylin. Using molecular dynamics simulations, we investigate how the equilibrium between amylin monomers in its functional form and fibrils associ...

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Autores principales: Chesney, Andrew D., Maiti, Buddhadev, Hansmann, Ulrich H.E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2023
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10077547/
https://www.ncbi.nlm.nih.gov/pubmed/37033831
http://dx.doi.org/10.1021/acsomega.3c00621
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author Chesney, Andrew D.
Maiti, Buddhadev
Hansmann, Ulrich H.E.
author_facet Chesney, Andrew D.
Maiti, Buddhadev
Hansmann, Ulrich H.E.
author_sort Chesney, Andrew D.
collection PubMed
description [Image: see text] COVID-19 can lead to the onset of type-II diabetes, which is associated with the aggregation of islet amyloid polypeptides, also called amylin. Using molecular dynamics simulations, we investigate how the equilibrium between amylin monomers in its functional form and fibrils associated with diabetes is altered in the presence of SARS-COV-2 protein fragments. For this purpose, we study the interaction between the fragment SFYVYSRVK of the envelope protein or the fragment FKNIDGYFKI of the spike protein with the monomer and two amylin fibril models. Our results are compared with earlier work studying such interactions for the two different proteins.
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spelling pubmed-100775472023-04-07 Human Amylin in the Presence of SARS-COV-2 Protein Fragments Chesney, Andrew D. Maiti, Buddhadev Hansmann, Ulrich H.E. ACS Omega [Image: see text] COVID-19 can lead to the onset of type-II diabetes, which is associated with the aggregation of islet amyloid polypeptides, also called amylin. Using molecular dynamics simulations, we investigate how the equilibrium between amylin monomers in its functional form and fibrils associated with diabetes is altered in the presence of SARS-COV-2 protein fragments. For this purpose, we study the interaction between the fragment SFYVYSRVK of the envelope protein or the fragment FKNIDGYFKI of the spike protein with the monomer and two amylin fibril models. Our results are compared with earlier work studying such interactions for the two different proteins. American Chemical Society 2023-03-23 /pmc/articles/PMC10077547/ /pubmed/37033831 http://dx.doi.org/10.1021/acsomega.3c00621 Text en © 2023 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 Chesney, Andrew D.
Maiti, Buddhadev
Hansmann, Ulrich H.E.
Human Amylin in the Presence of SARS-COV-2 Protein Fragments
title Human Amylin in the Presence of SARS-COV-2 Protein Fragments
title_full Human Amylin in the Presence of SARS-COV-2 Protein Fragments
title_fullStr Human Amylin in the Presence of SARS-COV-2 Protein Fragments
title_full_unstemmed Human Amylin in the Presence of SARS-COV-2 Protein Fragments
title_short Human Amylin in the Presence of SARS-COV-2 Protein Fragments
title_sort human amylin in the presence of sars-cov-2 protein fragments
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10077547/
https://www.ncbi.nlm.nih.gov/pubmed/37033831
http://dx.doi.org/10.1021/acsomega.3c00621
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