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

Hayden Peacock, Jinghui Luo, Tohru Yamashita, James Luccarelli, Sam Thompson, Andrew Hamilton

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)6435-6439
Number of pages5
JournalChemical Science
Volume7
Issue number10
DOIs
StatePublished - 2016

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Islet Amyloid Polypeptide
Scaffolds
Conformations
Molecules
Membrane Proteins
Protein folding
Pathology
Medical problems
Agglomeration
Proteins

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Non-covalent S⋯O interactions control conformation in a scaffold that disrupts islet amyloid polypeptide fibrillation. / Peacock, Hayden; Luo, Jinghui; Yamashita, Tohru; Luccarelli, James; Thompson, Sam; Hamilton, Andrew.

In: Chemical Science, Vol. 7, No. 10, 2016, p. 6435-6439.

Research output: Contribution to journalArticle

Peacock, Hayden ; Luo, Jinghui ; Yamashita, Tohru ; Luccarelli, James ; Thompson, Sam ; Hamilton, Andrew. / Non-covalent S⋯O interactions control conformation in a scaffold that disrupts islet amyloid polypeptide fibrillation. In: Chemical Science. 2016 ; Vol. 7, No. 10. pp. 6435-6439.
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