Core Viewpoint - The research reveals the atomic structure of pathological human islet amyloid polypeptide (hIAPP) fibrils, providing a significant foundation for understanding the mechanisms of type 2 diabetes (T2D) and developing treatment strategies [7]. Group 1: Research Findings - The study analyzed hIAPP fibrils extracted from pancreatic tissues of three T2D patients using cryo-electron microscopy (cryo-EM) [4]. - The hIAPP fibrils exhibited a uniform morphology, consisting of two symmetrical protofibrils, containing amino acid residues 2-37, and forming an Ω-shaped spatial fold [4]. - Additional electron density observed in pancreatic hIAPP fibrils suggests potential ligand binding, which may significantly impact the pathogenesis of T2D [4][5]. Group 2: Structural Insights - The core findings include the atomic structure of hIAPP fibrils derived from T2D patients [5]. - The hIAPP fibrils display an unprecedented Ω-shaped folding structure with a conserved core region [5]. - Structural similarities were observed between pathological hIAPP fibrils and Aβ fibrils [5].