The Two Peptides Fragments of Goat Milk CSN1S2 Protein Blocked Insulin Receptor to Interact Ligand: In Silico Study

Insulin is a hormone that plays important role for tissue development and glucose homeostasis, it has significant implications for many chronic diseases, especially diabetes mellitus (DM). Alpha casein S2 (CSN1S2) isolated from Ethawah goat's milk has eight peptides residue contain seven to twelve amino acid residues and has multiple functions, such as antimicrobial, immunomodulatory, and anti-oxidant. The purpose of this study is to observe the interaction between CSN1S2 protein peptides and Insulin Receptor. 3-D structure of Insulin Receptor is done by accessing RCSB PDB (ID: 4ZXB), protein was prepared using Discovery Studio BIOVIA 2019 and ligands were prepared using PyRx. Insulin receptor was docked to CSN1S2 protein peptides using HEX 8.0 software and visualized using Discovery Studio BIOVIA 2019. The results of this study showed different binding patterns, most of the chemistry bond were resulted between protein and ligands interaction are hydrogen bonds and electrostatic, the binding energy of CSN1S2 fragment 41-47 and fragment 214-221 to insulin receptor are -186.9 kJ/mol and -172.7 kJ/mol respectively. The caprine CSN1S2 protein peptides have ability to be used as therapeutic agents, such as DM because they can bind to specific sites of the insulin receptor and may reduce the insulin resistance mechanism.