Amylin (8-37) (human)

Amylin (8-37) (human) (hIAPP (8-37)) is a 8-37 fragment of human islet amyloid polypeptide (IAPP). The duplex folding structure in the Amylin (8-37) (human) assembly has a hairpin structure[1].

Research Areas >> Metabolic Disease

Human islet amyloid polypeptide (hIAPP, amylin) is a major component in pancreatic amyloid deposits. Human IAPP with 37 amino acid residues is known to form soluble aggregates that further assemble into protofibrils and mature fibrils and eventually develop into plagues, and many studies have been conducted to identify the core regions with amyloidogenic properties. The assembly structures of Amylin (8-37) (human) (hIAPP (8-37)) shows lamella structures. The C terminal strands of Amylin (8-37) (human) peptides are stabilized by the coassembly molecule 4Bpy[1].

[1]. Xiao-Bo Mao, et al. Beta structure motifs of islet amyloid polypeptides identified through surface-mediated assemblies. Proc Natl Acad Sci U S A. 2011 Dec 6;108(49):19605-10.