| Description | Islet amyloid polypeptide (IAPP) (also known as diabetes-associated peptide or amylin) is a pancreatic islet hormone that is stored with insulin in beta cell granules [ ]. IAPP has a propensity to form islet cell-disrupting amyloid deposits, and opposes the action of insulin in peripheral tissues; the peptide may therefore have a significant role in the development of Type 2 diabetes mellitus []. It is thought that an intrinsic structural motif of IAPP, which only occurs in species that develop age-associated or Type 2 diabetes (e.g., Homo sapiens (Human) and Felis silvestris catus (Cat)), is linked to its amyloidogenicity []. IAPP is a short, 37-residue peptide. The hormone selectively inhibits insulin-stimulated glucose utilisation and glycogen deposition in muscle, but does not affect adipocyte glucose metabolism. The sequences of amylin and the calcitonin gene-related peptides (CGRPs) show strong similarity: both peptides have a conserved N-terminal intramolecular disulphide bridge, and both have a C-terminal glycine, which suggests that the C-terminal residue of amylin, like that of CGRP, is amidated []. Near- and far-UV CD spectra of human alpha CGRP, analogues and fragments of CGRP, and amylin have been recorded in aqueous solution and in trifluoro- ethanol/water mixtures []. The peptides were shown to contain significant amounts of α-helix in aqueous solution, this amount increasing upon addition of TFE. Amylin appears to contain less helix than CGRP []. | Name | Islet amyloid polypeptide |
| Short Name | IAPP | Type | Family |
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