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Sequence-dependent aggregation-prone conformations of islet amyloid polypeptide

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Title
Sequence-dependent aggregation-prone conformations of islet amyloid polypeptide
Author(s)
Choi, Bumjoon; Kim, Nam Hyeong; Jin, Geun Young; Kim, Yung Sam; Yong Ho Kim; Eom, Kilho
Publication Date
2021-10-21
Journal
PHYSICAL CHEMISTRY CHEMICAL PHYSICS, v.23, no.39, pp.22532 - 22542
Publisher
ROYAL SOC CHEMISTRY
Abstract
Amyloid proteins, which aggregate to form highly ordered structures, play a crucial role in various disease pathologies. Despite many previous studies on amyloid fibrils, which are an end product of protein aggregation, the structural characteristics of amyloid proteins in the early stage of aggregation and their related aggregation mechanism still remain elusive. The role of the amino acid sequence in the aggregation-prone structures of amyloid proteins at such a stage is not understood. Here, we have studied the sequence-dependent structural characteristics of islet amyloid polypeptide based on atomistic simulations and spectroscopic experiments. We show that the amino acid sequence determines non-bonded interactions that play a leading role in the formation of aggregation-prone conformations. Specifically, a single point mutation critically changes the population of aggregation-prone conformations, resulting in a change of the aggregation mechanism. Our simulation results were supported by experimental results suggesting that mutation affects the kinetics of aggregation and the structural characteristics of amyloid aggregates. Our study provides an insight into the role of sequence-dependent aggregation-prone conformations in the underlying mechanisms of amyloid aggregation.
URI
https://pr.ibs.re.kr/handle/8788114/10540
DOI
10.1039/d1cp01061a
ISSN
1463-9076
Appears in Collections:
Center for Neuroscience Imaging Research (뇌과학 이미징 연구단) > 1. Journal Papers (저널논문)
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