Proteomic Analysis and Characterization of Amylin (IAPP) in Homo Sapiens

Abstract

Amylin which is also called as Islet amyloids polypeptide (IAPP), is a pancreatic B-cell hormone co-released with insulin. Amyloids are insoluble fiber and the abnormal accumulation of these fibers in the tissue of the pancreas leads to type II diabetes. Bioinformatics tools were applied to process, prioritise and annotate the raw sequence which is then converted into meaningful information about the proteins. These methods are useful in the medical research as they increase the annotation of proteome through functional and structural genomic efforts. Firstly, the result of primary structure analysis reveals that most of the amylin are hydrophobic in nature due to presence of high nonpolar residues content. Amylin has both acidic and basic property as its isoelectric point ranged from 5.31-9.83. The aliphatic index computed by Expasy’s Protparam infers that most of the amylin are stable at wide range of temperature (66.84-108.43). The secondary structure analysis by SOPMA reveals that amylin contain more random coils and beta sheets. SMART values revealed an expected range of 0.0000198-27. The Ligand binding site of an amylin was obtained by SWISS-MODEL as it determines the 3D structure of a protein. The RNA structure was predicted by using Genebee service software.