| dc.description.abstract | Dengue hemorrhagic fever (DHF) caused by the dengue virus is an endemic disease in
Indonesia. The dengue virus is transmitted to the human body by Aedes aegypti vector through the process
of blood feeding. The success of dengue virus transmission through blood feeding is due to the presence of
a protein that acts as an anti-coagulant, namely apyrase. Apyrase is an enzyme capable of degrading ADP
in the blood feeding process. ADP has an important role as an inducer in platelet aggregation process.
Therefore, our study aims to determine the strength of the interaction between Apyrase protein and ADP
substrate in its activity as an inhibitor of platelet aggregation during blood feeding. In silico analysis on
Apyrase and ADP ligands conducted by molecular docking method using AutoDock Vina software.
Apyrase sequences of Ae. aegypti was taken from the UniProt database with accession number P50635.
The three-dimensional structure of the ADP ligand was obtained from the PubChem database with
accession number 6022. The study showed that interaction of apyrase enzyme with ADP ligand has good
spontaneity based on the G value. The G value of these interaction are -9.6 kcal/mol (ADP sub unit 1) and
-9.4 kcal/mol (ADP sub unit 2). The docking analysis showed the interaction of the apyrase enzyme with
the ADP ligand bind exothermically. The active sites of the apyrase enzyme that interact with the ADP
ligand are on the the amino acids HIS-49, ASP-98, ASN-130, HIS-131, HIS-257, HIS-259, ARG-370,
GLU-451, ARG-453, and THR. -454. | en_US |
