Non-covalent S...O interactions control conformation in a scaffold that disrupts islet amyloid polypeptide fibrillation
Non-covalent S...O interactions control conformation in a scaffold that disrupts islet amyloid polypeptide fibrillation
Conformationally-constrained molecules that selectively recognise the surfaces of proteins have the potential to direct the path of protein folding. Such molecules are of therapeutic interest because the misfolding of proteins, especially that which results in fibrillation and aggregation, is strongly correlated with numerous diseases. Here we report the novel use of S?O interactions as a conformational control element in a new class of non-peptidic scaffold that mimics key elements of protein surfaces. These molecules disrupt the fibrillation of islet amyloid polypeptide (IAPP), a process that is implicated in the pathology of type II diabetes.
6435-6439
Peacock, Hayden
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Luo, Jinghui
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Yamashita, Tohru
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Luccarelli, James
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Thompson, Sam
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Hamilton, Andrew D.
048a6c75-91bf-4555-ab12-ce885eee65dd
1 July 2016
Peacock, Hayden
8db61484-88ba-430b-8e51-5cc2d6eb3cca
Luo, Jinghui
d9dcd354-dcbb-4153-903f-3694c522374c
Yamashita, Tohru
1fb50b71-f393-48b4-8707-27cbb7a22958
Luccarelli, James
9afdfaf8-5c48-4110-a281-2eeeabb6c2ff
Thompson, Sam
99b7e34e-fe24-401c-b7b0-64e56cbbbcb1
Hamilton, Andrew D.
048a6c75-91bf-4555-ab12-ce885eee65dd
Peacock, Hayden, Luo, Jinghui, Yamashita, Tohru, Luccarelli, James, Thompson, Sam and Hamilton, Andrew D.
(2016)
Non-covalent S...O interactions control conformation in a scaffold that disrupts islet amyloid polypeptide fibrillation.
Chemical Science, 7 (10), .
(doi:10.1039/c6sc00756b).
Abstract
Conformationally-constrained molecules that selectively recognise the surfaces of proteins have the potential to direct the path of protein folding. Such molecules are of therapeutic interest because the misfolding of proteins, especially that which results in fibrillation and aggregation, is strongly correlated with numerous diseases. Here we report the novel use of S?O interactions as a conformational control element in a new class of non-peptidic scaffold that mimics key elements of protein surfaces. These molecules disrupt the fibrillation of islet amyloid polypeptide (IAPP), a process that is implicated in the pathology of type II diabetes.
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Accepted/In Press date: 9 May 2016
e-pub ahead of print date: 1 July 2016
Published date: 1 July 2016
Organisations:
Chemical Biology Group
Identifiers
Local EPrints ID: 402307
URI: http://eprints.soton.ac.uk/id/eprint/402307
ISSN: 1478-6524
PURE UUID: dc147387-b87c-45de-884f-72b5dd820365
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Date deposited: 04 Nov 2016 15:32
Last modified: 15 Mar 2024 03:54
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Contributors
Author:
Hayden Peacock
Author:
Jinghui Luo
Author:
Tohru Yamashita
Author:
James Luccarelli
Author:
Andrew D. Hamilton
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