The Complexity of Molecular Interactions and Bindings between Cyclic Peptide and Inhibit Polymerase A and B1 (PAC-PB1N) H1N1

TL;DR

This study uses computational modeling to analyze how cyclic peptides interact with the H1N1 virus enzyme PAC-PB1N, exploring their potential as new antiviral drug candidates amid high viral mutation rates.

Contribution

It introduces a computational approach to evaluate cyclic peptides as inhibitors of H1N1 polymerase, providing insights into their molecular interactions.

Findings

Cyclic peptides CKTTC and CKKTC show potential binding to PAC-PB1N.

Molecular modeling reveals specific amino acid interactions.

The approach supports cyclic peptides as promising drug candidates.

Abstract

The influenza/H1N1 virus has caused hazard in the public health of many countries. Hence, existing influenza drugs could not cope with H1N1 infection due to the high mutation rate of the virus. In this respect, new method to block the virus was devised. The polymerase PAC-PB1N enzyme is responsible for the replication of H1N1 virus. Thus, novel inhibitors were developed to ward off the functionality of the enzyme. In this research, cyclic peptides has been chosen to inhibit PAC-PB1N due to its proven stability in reaching the drug target. Thus, computational method for elucidating the molecular interaction between cyclic peptides and PAC-PB1N has been developed by using the LigX tools from MOE 2008.10 software. The tools could render the bindings that involved in the interactions. The interactions between individual amino acid in the inhibitor and enzyme could be seen as well. Thus, the peptide sequences of CKTTC and CKKTC were chosen as the lead compounds. In this end, the feasibility of cyclic peptides to act as drug candidate for H1N1 could be exposed by the 2d and 3d modeling of the molecular interactions.