Identification of novel ligands for inhibition of mutant Q43R islet amyloid polypeptide (IAPP) using In-silico docking

• Main Authors: Viswateja Reddy, Dorankula, John, Arun
• Format: Conference Proceeding
• Language: English
• Subjects: Affinity; Binding; Biological activity; Biological properties; Ligands; Polypeptides; Proteins
• ISSN: 0094-243X; 1551-7616
• DOI: 10.1063/5.0233039

New ligands that inhibit mutant Q43R IAPP are the focus of this study, which use in-silico docking to find them (islet amyloid polypeptide). Both the Procedures and the Materials: Within the scope of this inquiry, we made use of Pymol as a visualizer in order to bring about mutagenization. Our docking tool of choice was PyRx, which allowed us to determine the binding affinities of a number of different ligands with the protein that we were interested in. LigPlus was utilised in order to do additional research on the interactions between the protein-ligand complex. As opposed to the MOLINSPIRATION tool, which was used to research biological activity, the AdmetSAR tool was utilised to investigate ADMET properties. Phosphatidylserine was found to have the potential to act as a ligand for the IAPP protein associated with the Q43R mutation, as demonstrated by the findings. At the end of the day, we came to the conclusion that PyRx was used to evaluate the binding affinities of the various ligands against the Q43R mutant IAPP. The strongest and most stable connections are formed with macromolecules by phosphatidylserine, which attaches to them with incredible affinity. In light of the further ADMET property investigation, the prospective ligand is now subject to the lipinski rule.