Copper(II) inhibits the formation of amylin amyloid in vitro.
The amyloidogenic peptide amylin is found associated with pancreatic islet beta-cells and is implicated in the aetiology of type-2 diabetes mellitus. We have used fluorimetry and transmission electron microscopy to investigate in vitro the influence of Al(III), Fe(III), Zn(II) and Cu(II) on amylin amyloid formation under near-physiological conditions. Cu(II) at 10.0 microM inhibited amylin of 0.4 and 2.0 microM from forming amyloid fibrils while the same concentration of either Al(III) or Zn(II) promoted the formation of beta-pleated sheet structures. If amylin amyloid is cytotoxic to beta-cells then Cu(II) should protect against the degeneration of the islets in type-2 diabetes mellitus.
Ward
Benjamin
B
School of Medicine, Keele University, Staffordshire ST5 5BG, UK.
Walker
Karen
K
Exley
Christopher
C
D000535:Aluminum / Q000737:chemistry / Q000494:pharmacology; D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism; D003300:Copper / Q000737:chemistry* / Q000494:pharmacology; D003924:Diabetes Mellitus, Type 2 / Q000378:metabolism; D005296:Ferrous Compounds / Q000737:chemistry / Q000494:pharmacology; D006801:Humans; D050417:Insulin-Secreting Cells / Q000378:metabolism; D058228:Islet Amyloid Polypeptide; D046529:Microscopy, Electron, Transmission; D015032:Zinc / Q000737:chemistry / Q000494:pharmacology
D000682:Amyloid; D005296:Ferrous Compounds; D058228:Islet Amyloid Polypeptide; D003300:Copper; D000535:Aluminum; D015032:Zinc