Premium
Small‐Molecule Inhibitors of Islet Amyloid Polypeptide Fibril Formation
Author(s) -
Mishra Rajesh,
Bulic Bruno,
Sellin Daniel,
Jha Suman,
Waldmann Herbert,
Winter Roland
Publication year - 2008
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200705372
Subject(s) - amylin , islet , small molecule , amyloid (mycology) , fibril , amyloid fibril , chemistry , protein aggregation , biochemistry , diabetes mellitus , biophysics , endocrinology , medicine , disease , biology , amyloid β , inorganic chemistry
Small and effective : The pathological aggregation of amylin (IAPP), which leads to type II diabetes mellitus, is effectively inhibited by small‐molecule rhodanine‐based inhibitors at nanomolar concentrations. The prevention of aggregation by treatment with the inhibitor is demonstrated by AFM (see image).