Journal article
Non-covalent S⋯O interactions control conformation in a scaffold that disrupts islet amyloid polypeptide fibrillation
- Abstract:
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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
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(Version of record, pdf, 1.4MB)
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- Publisher copy:
- 10.1039/C6SC00756B
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Authors
Funding
University of Oxford
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Bibliographic Details
- Publisher:
- Royal Society of Chemistry Publisher's website
- Journal:
- Chemical Science Journal website
- Publication date:
- 2016-07-01
- Acceptance date:
- 2016-05-09
- DOI:
- EISSN:
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2041-6539
- ISSN:
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2041-6520
- Source identifiers:
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632214
Item Description
- Pubs id:
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pubs:632214
- UUID:
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uuid:1c5a92d8-e487-4934-8841-b72656b567ca
- Local pid:
- pubs:632214
- Deposit date:
- 2016-07-06
Terms of use
- Copyright holder:
- Royal Society of Chemistry
- Copyright date:
- 2016
- Notes:
- Author(s) retain copyright; published by the Royal Society of Chemistry under license. This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence.
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