In silico study of the interaction between serotonin and D7 protein from the salivary gland of Aedes aegypti

Protein components of the salivary glands of disease vectors have been known to facilitate the blood-feeding process in the host body. The main component of the salivary glands of Aedes aegypti is the immunogenic D7 protein. During the blood-feeding process, the D7 protein can bind to biogenic amine compounds, such as serotonin, which is a neurotransmitter involved in platelet activation. This ability indicates that the D7 protein can inhibit the platelet aggregation process. This study aims to explore in silico the interaction between serotonin and the D7 protein from the salivary glands of Ae. aegypti using a molecular docking approach. The methods used in this study include the selection of the 3D structure of the D7 protein and serotonin ligand, preparation of the 3D structure of the D7 protein, native ligands, and test ligands, validation of the molecular docking method, and analysis and visualization of the molecular docking results. The results of molecular docking between the D7 protein and the serotonin ligand showed a ∆G value for the interaction of −9.25 kcal/mol. The serotonin ligand binds to the active site of the D7 protein through several amino acid residues, including GLU 158, ILE 175, ARG 176, TYR 178, TYR 248, ASP 265, and GLU 268. These amino acid residues of the D7 protein bind to atoms on the serotonin ligand through conventional hydrogen bonds, carbon hydrogen bonds, π-σ bonds, π-π T-shaped bonds, and π-alkyl bonds. Based on the in silico data, it is shown that the D7 protein from the salivary glands of Ae. aegypti can bind stably and spontaneously to serotonin ligands. This indicates that the D7 protein has potential as a platelet aggregation inhibitor agent for the development of drug discovery in the fields of health and pharmacy.