Amylin, also called islet amyloid polypeptide (IAPP), is a 37-amino-acid hormone co-secreted with insulin from pancreatic beta-cells in roughly a 1:100 molar ratio. It carries a disulfide bridge between residues 2 and 7 and a C-terminal amide, both required for activity.
Receptors and reported biology
Amylin does not have a dedicated single receptor. It acts at amylin receptors formed when the calcitonin receptor associates with receptor activity-modifying proteins (RAMP1–3), producing the AMY1–AMY3 subtypes, with signalling concentrated in the area postrema and nucleus tractus solitarius. Published work describes slowed gastric emptying, suppression of postprandial glucagon, and meal-ending satiation signalling — a pathway distinct from GLP-1, which is the rationale for studying the two together.
The aggregation problem
Human amylin is strongly amyloidogenic; it self-assembles into fibrils, which is both a feature of islet pathology in type 2 diabetes and a formulation obstacle. Analogs solve it by sequence change — pramlintide substitutes prolines from the non-aggregating rat sequence, and cagrilintide is a long-acting acylated analog studied alongside semaglutide in combination research.
Related terms
incretin · disulfide bridge. See the amylin research family, Semaglutide + Cagrilintide, and Cagrilintide vs Semaglutide.