Non-covalent S···O interactions control conformation in a scaffold that disrupts islet amyloid polypeptide fibrillation.
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ABSTRACT:
SUBMITTER: Peacock H
PROVIDER: S-EPMC5363787 | biostudies-literature | 2016 Oct
REPOSITORIES: biostudies-literature
Publications
Non-covalent S···O interactions control conformation in a scaffold that disrupts islet amyloid polypeptide fibrillation.
Peacock Hayden H Luo Jinghui J Yamashita Tohru T Luccarelli James J Thompson Sam S Hamilton Andrew D AD
Chemical science 20160701 10
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 ...[more]
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