Ontology highlight
ABSTRACT:
SUBMITTER: Kakinen A
PROVIDER: S-EPMC6162064 | biostudies-literature | 2018 Jul
REPOSITORIES: biostudies-literature
Nano research 20180701 7
Understanding how small molecules interface amyloid fibrils on the nanoscale is of importance for developing therapeutic treatment against amyloid-based diseases. Here we show, for the first time, that human islet amyloid polypeptide (IAPP) in the fibrillar form is polymorphic and ambidextrous possessing multiple periodicities. Upon interfacing with small molecule epigallocatechin gallate (EGCG), IAPP aggregation was rendered off pathway assuming the form of soft and disordered clusters, while m ...[more]