Effect of Copper-Catalyzed Oxidation on the Aggregation of the Islet Amyloid Polypeptide.

ABSTRACT: The islet amyloid polypeptide (IAPP) is a 37-residue peptide hormone secreted by pancreatic β-cells that is known to aggregate into amyloid fibrils. These fibrils accumulate in the pancreatic islets of individuals afflicted with type 2 diabetes and are implicated in β-cell dysfunction. Metal ions such as copper and zinc are known to modulate IAPP fibrillization, yet the role of metal-induced oxidative modifications in this process remains largely unexplored. This study examines the non-enzymatic post-translational oxidation of IAPP and its effects on aggregation using the biologically relevant Cu/O₂/ascorbate system. Mass spectrometry identified residues within the amyloidogenic region (residues 20-29) as the primary targets of oxidation. These oxidative modifications impaired t

SUBMITTER: Amilca O 

PROVIDER: S-EPMC12649479 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature