Issue 10, 2016

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

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

Supplementary files

Article information

Article type
Edge Article
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
Creative Commons BY-NC license

Chem. Sci., 2016,7, 6435-6439

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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