Interconversion between Serum Amyloid A Native and Fibril Conformations

[Image: see text] Overexpression of serum amyloid A (SAA) can lead to a form of amyloidosis where the fibrils are made of SAA fragments, most often SAA(1–76). Using Replica Exchange with Tunneling, we study the conversion of a SAA(1–76) chain between the folded conformation and a fibril conformation...

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Autores principales: Yasar, Fatih, Sheridan, Miranda S., Hansmann, Ulrich H. E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2022
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9016813/
https://www.ncbi.nlm.nih.gov/pubmed/35449919
http://dx.doi.org/10.1021/acsomega.2c00566
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author Yasar, Fatih
Sheridan, Miranda S.
Hansmann, Ulrich H. E.
author_facet Yasar, Fatih
Sheridan, Miranda S.
Hansmann, Ulrich H. E.
author_sort Yasar, Fatih
collection PubMed
description [Image: see text] Overexpression of serum amyloid A (SAA) can lead to a form of amyloidosis where the fibrils are made of SAA fragments, most often SAA(1–76). Using Replica Exchange with Tunneling, we study the conversion of a SAA(1–76) chain between the folded conformation and a fibril conformation. We find that the basins in the free energy landscape corresponding to the two motifs are separated by barriers of only about 2–3 k(B)T. Crucial for the assembly into the fibril structure is the salt bridge 26E–34K that provides a scaffold for forming the fibril conformation.
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spelling pubmed-90168132022-04-20 Interconversion between Serum Amyloid A Native and Fibril Conformations Yasar, Fatih Sheridan, Miranda S. Hansmann, Ulrich H. E. ACS Omega [Image: see text] Overexpression of serum amyloid A (SAA) can lead to a form of amyloidosis where the fibrils are made of SAA fragments, most often SAA(1–76). Using Replica Exchange with Tunneling, we study the conversion of a SAA(1–76) chain between the folded conformation and a fibril conformation. We find that the basins in the free energy landscape corresponding to the two motifs are separated by barriers of only about 2–3 k(B)T. Crucial for the assembly into the fibril structure is the salt bridge 26E–34K that provides a scaffold for forming the fibril conformation. American Chemical Society 2022-03-30 /pmc/articles/PMC9016813/ /pubmed/35449919 http://dx.doi.org/10.1021/acsomega.2c00566 Text en © 2022 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 Yasar, Fatih
Sheridan, Miranda S.
Hansmann, Ulrich H. E.
Interconversion between Serum Amyloid A Native and Fibril Conformations
title Interconversion between Serum Amyloid A Native and Fibril Conformations
title_full Interconversion between Serum Amyloid A Native and Fibril Conformations
title_fullStr Interconversion between Serum Amyloid A Native and Fibril Conformations
title_full_unstemmed Interconversion between Serum Amyloid A Native and Fibril Conformations
title_short Interconversion between Serum Amyloid A Native and Fibril Conformations
title_sort interconversion between serum amyloid a native and fibril conformations
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9016813/
https://www.ncbi.nlm.nih.gov/pubmed/35449919
http://dx.doi.org/10.1021/acsomega.2c00566
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