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...
Main Authors: | , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2015-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC4551895?pdf=render |
id |
doaj-c878ede8d8384efbae2477ce20066723 |
---|---|
record_format |
Article |
spelling |
doaj-c878ede8d8384efbae2477ce200667232020-11-25T02:04:37ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01108e013660210.1371/journal.pone.0136602pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils.Tomas SneiderisDomantas DarguzisAkvile BotyriuteMartynas GrigaliunasRoland WinterVytautas SmirnovasPrions 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.http://europepmc.org/articles/PMC4551895?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Tomas Sneideris Domantas Darguzis Akvile Botyriute Martynas Grigaliunas Roland Winter Vytautas Smirnovas |
spellingShingle |
Tomas Sneideris Domantas Darguzis Akvile Botyriute Martynas Grigaliunas Roland Winter Vytautas Smirnovas pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils. PLoS ONE |
author_facet |
Tomas Sneideris Domantas Darguzis Akvile Botyriute Martynas Grigaliunas Roland Winter Vytautas Smirnovas |
author_sort |
Tomas Sneideris |
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. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2015-01-01 |
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. |
url |
http://europepmc.org/articles/PMC4551895?pdf=render |
work_keys_str_mv |
AT tomassneideris phdrivenpolymorphismofinsulinamyloidlikefibrils AT domantasdarguzis phdrivenpolymorphismofinsulinamyloidlikefibrils AT akvilebotyriute phdrivenpolymorphismofinsulinamyloidlikefibrils AT martynasgrigaliunas phdrivenpolymorphismofinsulinamyloidlikefibrils AT rolandwinter phdrivenpolymorphismofinsulinamyloidlikefibrils AT vytautassmirnovas phdrivenpolymorphismofinsulinamyloidlikefibrils |
_version_ |
1724942194917244928 |