Ontology highlight
ABSTRACT:
SUBMITTER: Wang Y
PROVIDER: S-EPMC7532939 | biostudies-literature | 2017 Aug
REPOSITORIES: biostudies-literature
Wang Yilin Y Kreutzer Adam G AG Truex Nicholas L NL Nowick James S JS
The Journal of organic chemistry 20170714 15
Aggregation of the islet amyloid polypeptide (IAPP) to form fibrils and oligomers is important in the progression of type 2 diabetes. This article describes X-ray crystallographic and solution-state NMR studies of peptides derived from residues 11-17 of IAPP that assemble to form tetramers. Incorporation of residues 11-17 of IAPP (RLANFLV) into a macrocyclic β-sheet peptide results in a monomeric peptide that does not self-assemble to form oligomers. Mutation of Arg<sub>11</sub> to the uncharged ...[more]