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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 protei...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1039/C6SC00756B

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Role:
Author
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University of Oxford More from this funder
Publisher:
Royal Society of Chemistry Publisher's website
Journal:
Chemical Science Journal website
Publication date:
2016-07-01
DOI:
EISSN:
2041-6539
ISSN:
2041-6520
URN:
uuid:1c5a92d8-e487-4934-8841-b72656b567ca
Source identifiers:
632214
Local pid:
pubs:632214

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