Abstract

IN SILICO STUDY OF ANTICANCER MECHANISM OF THE MARINE BIOACTIVE COMPOUND TALTOBULIN

Danni Ramdhani* and Sri Agung Fitri Kusuma

Abstract

Objective: Taltobulin, a synthetic counterpart of hemiasterlin, was first obtained from the marine sponge Hemiasterella minor, with potential antimitotic and antineoplastic activities. The principal objective of this study is to employ the molecular docking approach to ascertain the mechanism responsible for Taltobulin's anticancer action. Vascular Endothelial Growth Factor Receptor-2 (VEGFR2), Procaspase7 (Pro7), and Protein Kinase B (PKB) are three different receptors with significant anticancer activities that were exploited in this computational investigation. Materials and Methods: Molecular docking was completed using Pyrx and autodock Vina in the computational chemistry method. The outcomes were displayed in the discovery studio program's two-dimensional interfaces. Affinity for binding score values and the kind of chemical bond that forms between the ligand and target receptor were assessed during the docking evaluation process. Results: The results of the PKB, VEGFR2, and Procaspase 7 docking analyses were -6.2 kcal/mol, -6.8 kcal/mol, and – 7.3 kcal/mol, respectively. Conclusion: Taltobulin's binding affinity score indicates dominant anticancer activity via procaspase7 in comparison to the native ligand-receptor.

Keywords: molecular docking, taltobulin, Hemiasterella minor, anticancer, binding affinity, protein kinase B, VEGFR2, procaspase7.