Author:
Wathon Syubbanul,Oktarianti Rike,Senjarini Kartika
Abstract
The salivary glands of mosquitoes contain protein molecules that facilitate blood-feeding. One important protein in Aedes aegypti (Ae. aegypti) salivary glands is the D7 protein, which is known to inhibit platelet aggregation by binding to leukotriene A4 molecules upon blood-feeding. Leukotriene A4 is known as a molecule that improves platelet aggregation. This ability to bind to leukotriene A4 demonstrates the potential of a new thrombolytic agent. This can be investigated through an in-silico study using the molecular docking method. The present study involved the 3D structure of the D7 protein and the Leukotriene A4 ligand. It also comprised preparing their structures, validating the molecular docking method, and analyzing the outcomes. The result of the molecular docking documented an ΔG value of 6.63 kcal/mol, which signified stable and spontaneous binding between the D7 protein and the leukotriene A4. The active site of the D7 protein when binding to the leukotriene A4 ligand involves several amino acid residues, namely GLN 177, TYR 178, ARG 176, VAL 193, ILE 175, MET 194, PHE 154, PHE 186, HIS 189, TYR 248 and PHE 264. The ability to bind to leukotriene A4, as an inducer of platelet aggregation, evidences the potential as a novel thrombolytic agent.