Lipid Membranes Influence the Ability of Small Molecules To Inhibit Huntingtin Fibrillization.

ABSTRACT: Several diseases, including Alzheimer's disease, Parkinson's disease, and Huntington's disease (HD), are associated with specific proteins aggregating and depositing within tissues and/or cellular compartments. The aggregation of these proteins is characterized by the formation of extended, β-sheet rich fibrils, termed amyloid. In addition, a variety of other aggregate species also form, including oligomers and protofibrils. Specifically, HD is caused by the aggregation of the huntingtin (htt) protein that contains an expanded polyglutamine domain. Due to the link between protein aggregation and disease, small molecule aggregation inhibitors have been pursued as potential therapeutic agents. Two such small molecules are epigallocatechin 3-gallate (EGCG) and curcumin, both of which inhibit

SUBMITTER: Beasley M 

PROVIDER: S-EPMC7778521 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature