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Issue 10, 2016
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Non-covalent S⋯O interactions control conformation in a scaffold that disrupts islet amyloid polypeptide fibrillation

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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.

Graphical abstract: Non-covalent S⋯O interactions control conformation in a scaffold that disrupts islet amyloid polypeptide fibrillation

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Supplementary files

Article information


Submitted
18 Feb 2016
Accepted
09 May 2016
First published
01 Jul 2016

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2016,7, 6435-6439
Article type
Edge Article

Non-covalent S⋯O interactions control conformation in a scaffold that disrupts islet amyloid polypeptide fibrillation

H. Peacock, J. Luo, T. Yamashita, J. Luccarelli, S. Thompson and A. D. Hamilton, Chem. Sci., 2016, 7, 6435 DOI: 10.1039/C6SC00756B

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