Ruthenium complexes as novel inhibitors of human islet amyloid polypeptide fibril formation.
Human islet amyloid polypeptide (hIAPP) can be linked to the pathology of type II diabetes. In this study, aromatic ring-containing Ru complexes were found to effectively inhibit the fibril formation of hIAPP and promote the disaggregation of formed fibrils by remarkably changing the β-sheet components.
Department of Chemistry, Renmin University of China, Beijing, 100872, China. whdu@chem.ruc.edu.cn.
Lei
L
He
Xuesong
X
Wang
Cong
C
Zhao
Hongfei
H
Wang
Weihong
W
Du
D000595:Amino Acid Sequence; D000682:Amyloid / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism; D056831:Coordination Complexes / Q000737:chemistry / Q000494:pharmacology*; D006801:Humans; D058228:Islet Amyloid Polypeptide / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary / Q000187:drug effects; D012428:Ruthenium / Q000737:chemistry / Q000494:pharmacology*
D000682:Amyloid; D056831:Coordination Complexes; D058228:Islet Amyloid Polypeptide; D012428:Ruthenium