Ontology highlight
ABSTRACT:
SUBMITTER: Rodriguez Camargo DC
PROVIDER: S-EPMC8591229 | biostudies-literature | 2021
REPOSITORIES: biostudies-literature
Rodriguez Camargo Diana C DC Chia Sean S Menzies Joseph J Mannini Benedetta B Meisl Georg G Lundqvist Martin M Pohl Christin C Bernfur Katja K Lattanzi Veronica V Habchi Johnny J Cohen Samuel Ia SI Knowles Tuomas P J TPJ Vendruscolo Michele M Linse Sara S
Frontiers in molecular biosciences 20211101
The aggregation of the human islet amyloid polypeptide (IAPP) is associated with diabetes type II. A quantitative understanding of this connection at the molecular level requires that the aggregation mechanism of IAPP is resolved in terms of the underlying microscopic steps. Here we have systematically studied recombinant IAPP, with amidated C-terminus in oxidised form with a disulphide bond between residues 3 and 7, using thioflavin T fluorescence to monitor the formation of amyloid fibrils as ...[more]