pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils

Prions are infective proteins, which can self-assemble into different strain conformations, leading to different disease phenotypes. An increasing number of studies suggest that prion-like self-propagation may be a common feature of amyloid-like structures. Thus it is important to unravel every poss...

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Main Authors:	Sneideris, Tomas, Darguzis, Domantas, Botyriute, Akvile, Grigaliunas, Martynas, Winter, Roland, Smirnovas, Vytautas
Format:	Online
Language:	English
Published:	Public Library of Science 2015
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4551895/

id	pubmed-4551895
recordtype	oai_dc
spelling	pubmed-45518952015-09-01 pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils Sneideris, Tomas Darguzis, Domantas Botyriute, Akvile Grigaliunas, Martynas Winter, Roland Smirnovas, Vytautas Research Article Prions are infective proteins, which can self-assemble into different strain conformations, leading to different disease phenotypes. An increasing number of studies suggest that prion-like self-propagation may be a common feature of amyloid-like structures. Thus it is important to unravel every possible factor leading to the formation of different amyloid strains. Here we report on the formation of two types of insulin amyloid-like fibrils with distinct infrared spectroscopic features grown under slightly different pH conditions. Similar to prion strains, both insulin fibril types are able to self-propagate their conformational template under conditions, favoring spontaneous formation of different type fibrils. The low-pH-induced insulin amyloid strain is structurally very similar to previously reported strains formed either in the presence of 20% ethanol, or by modification of the amino acid sequence of insulin. A deeper analysis of literature data in the context of our current findings suggests a shift of the monomer-dimer equilibrium of insulin as a possible factor controlling the formation of different strains. Public Library of Science 2015-08-27 /pmc/articles/PMC4551895/ /pubmed/26313643 http://dx.doi.org/10.1371/journal.pone.0136602 Text en © 2015 Sneideris et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Sneideris, Tomas Darguzis, Domantas Botyriute, Akvile Grigaliunas, Martynas Winter, Roland Smirnovas, Vytautas
spellingShingle	Sneideris, Tomas Darguzis, Domantas Botyriute, Akvile Grigaliunas, Martynas Winter, Roland Smirnovas, Vytautas pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils
author_facet	Sneideris, Tomas Darguzis, Domantas Botyriute, Akvile Grigaliunas, Martynas Winter, Roland Smirnovas, Vytautas
author_sort	Sneideris, Tomas
title	pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils
title_short	pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils
title_full	pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils
title_fullStr	pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils
title_full_unstemmed	pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils
title_sort	ph-driven polymorphism of insulin amyloid-like fibrils
description	Prions are infective proteins, which can self-assemble into different strain conformations, leading to different disease phenotypes. An increasing number of studies suggest that prion-like self-propagation may be a common feature of amyloid-like structures. Thus it is important to unravel every possible factor leading to the formation of different amyloid strains. Here we report on the formation of two types of insulin amyloid-like fibrils with distinct infrared spectroscopic features grown under slightly different pH conditions. Similar to prion strains, both insulin fibril types are able to self-propagate their conformational template under conditions, favoring spontaneous formation of different type fibrils. The low-pH-induced insulin amyloid strain is structurally very similar to previously reported strains formed either in the presence of 20% ethanol, or by modification of the amino acid sequence of insulin. A deeper analysis of literature data in the context of our current findings suggests a shift of the monomer-dimer equilibrium of insulin as a possible factor controlling the formation of different strains.
publisher	Public Library of Science
publishDate	2015
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4551895/
_version_	1613469846799908864

pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils

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