pH-controlled stacking direction of the β-strands in peptide fibrils

Abstract Peptides provide a framework for generating functional biopolymers. In this study, the pH-dependent structural changes in the 21–29 fragment peptide of β2-microglobulin (β2m21–29) during self-aggregation, i.e., the formation of an amyloid fibril, were discussed. The β-sheet structures forme...

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Autores principales:	Wei-Hsuan Tseng, Szu-Hua Chen, Hirotsugu Hiramatsu
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/686b8df65ca945c899c8cea45c469a4f
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spelling	oai:doaj.org-article:686b8df65ca945c899c8cea45c469a4f2021-12-02T12:40:41ZpH-controlled stacking direction of the β-strands in peptide fibrils10.1038/s41598-020-79001-x2045-2322https://doaj.org/article/686b8df65ca945c899c8cea45c469a4f2020-12-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-79001-xhttps://doaj.org/toc/2045-2322Abstract Peptides provide a framework for generating functional biopolymers. In this study, the pH-dependent structural changes in the 21–29 fragment peptide of β2-microglobulin (β2m21–29) during self-aggregation, i.e., the formation of an amyloid fibril, were discussed. The β-sheet structures formed during parallel stacking under basic conditions (pH ≥ 7.7) adopted an anti-parallel stacking configuration under acidic conditions (pH ≤ 7.6). The parallel and anti-parallel β-sheets existed separately at the intermediate pH (pH = 7.6–7.7). These results were attributed to the rigidity of the β-sheets in the fibrils, which prevented the stable hydrogen bonding interactions between the parallel and anti-parallel β-sheet moieties. This observed pH dependence was ascribed to two phenomena: (i) the pH-dependent collapse of the β2m21–29 fibrils, which consisted of 16 ± 3 anti-parallel β-sheets containing a total of 2000 β-strands during the deprotonation of the NH3 + group (pK a = 8.0) of the β-strands that occurred within 0.7 ± 0.2 strands of each other and (ii) the subsequent formation of the parallel β-sheets. We propose a framework for a functional biopolymer that could alternate between the two β-sheet structures in response to pH changes.Wei-Hsuan TsengSzu-Hua ChenHirotsugu HiramatsuNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 10, Iss 1, Pp 1-9 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Wei-Hsuan Tseng Szu-Hua Chen Hirotsugu Hiramatsu pH-controlled stacking direction of the β-strands in peptide fibrils
description	Abstract Peptides provide a framework for generating functional biopolymers. In this study, the pH-dependent structural changes in the 21–29 fragment peptide of β2-microglobulin (β2m21–29) during self-aggregation, i.e., the formation of an amyloid fibril, were discussed. The β-sheet structures formed during parallel stacking under basic conditions (pH ≥ 7.7) adopted an anti-parallel stacking configuration under acidic conditions (pH ≤ 7.6). The parallel and anti-parallel β-sheets existed separately at the intermediate pH (pH = 7.6–7.7). These results were attributed to the rigidity of the β-sheets in the fibrils, which prevented the stable hydrogen bonding interactions between the parallel and anti-parallel β-sheet moieties. This observed pH dependence was ascribed to two phenomena: (i) the pH-dependent collapse of the β2m21–29 fibrils, which consisted of 16 ± 3 anti-parallel β-sheets containing a total of 2000 β-strands during the deprotonation of the NH3 + group (pK a = 8.0) of the β-strands that occurred within 0.7 ± 0.2 strands of each other and (ii) the subsequent formation of the parallel β-sheets. We propose a framework for a functional biopolymer that could alternate between the two β-sheet structures in response to pH changes.
format	article
author	Wei-Hsuan Tseng Szu-Hua Chen Hirotsugu Hiramatsu
author_facet	Wei-Hsuan Tseng Szu-Hua Chen Hirotsugu Hiramatsu
author_sort	Wei-Hsuan Tseng
title	pH-controlled stacking direction of the β-strands in peptide fibrils
title_short	pH-controlled stacking direction of the β-strands in peptide fibrils
title_full	pH-controlled stacking direction of the β-strands in peptide fibrils
title_fullStr	pH-controlled stacking direction of the β-strands in peptide fibrils
title_full_unstemmed	pH-controlled stacking direction of the β-strands in peptide fibrils
title_sort	ph-controlled stacking direction of the β-strands in peptide fibrils
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/686b8df65ca945c899c8cea45c469a4f
work_keys_str_mv	AT weihsuantseng phcontrolledstackingdirectionofthebstrandsinpeptidefibrils AT szuhuachen phcontrolledstackingdirectionofthebstrandsinpeptidefibrils AT hirotsuguhiramatsu phcontrolledstackingdirectionofthebstrandsinpeptidefibrils
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pH-controlled stacking direction of the β-strands in peptide fibrils

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