In silico structural biology studies between Aspirin and the CFTR (Cystic fibrosis transmembrane conductance regulator) proteins of the orthologous species, Homo sapiens and Pongo abelii for the control of Cystic Fibrosis

Abstract

The respiratory and digestive systems are the main organs affected by the complicated hereditary disease known as cystic fibrosis (CF). The CFTR protein becomes defective as a result of mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene. In order to make the CFTR protein of both species interact with the anti-inflammatory medication aspirin, we selected the human and Pongo abelii (Sumatran orangutan) sequence homology for this study. To investigate its interactions with aspirin, the mutant CFTR-Human (Cystic Fibrosis Transmembrane conductance Regulator) and CFTR of Pongo abelii were acquired from the UniProt database. Aspirin and CFTR binding affinities can be found using CB Dock, an automated drug docking server. It is possible to clarify the whole 3D H-bond interactions and structural details. It is clear from the docking study results that aspirin directly binds to the functional motif areas of both species' CFTR. Aspirin and CFTR's electrostatic interaction is shown in three dimensions using concepts from molecular dynamics techniques. Finally, it may be said that the anti-inflammatory drug aspirin aids in the prevention of cystic fibrosis. Our objective is to present an example of the molecular mechanism by which aspirin interacts with CFTR. By examining the relationship between human cystic fibrosis and Pongo abelii's interaction with CFTR, pharmacological research studies in humans can be carried out.