Structural Insights into Benzothiazole Derivatives as Modulators of Dehaloperoxidase: A Docking Study

Abstract

The aims of this work are the investigation of the docking interactions between DHP from Amphitrite ornata and a set of BTZ compounds to elucidate the effect of alterations in the chemical structure of the ligand on binding affinity. The docking results show the ability of binding strength from compound BTZ (-3.6) to BTZ-AC (-6.2). The improved binding shown in BTZ-M, BTZ-P, and BTZ-AC is due to the presence of extra van der Waals contacts and hydrogen interactions with critical residues including K58, L62, and V59. Here, again, polar interaction demonstrated a higher interaction energy than hydrophobic interaction, and BTZ-AC emerged as the best interacting ligand due to the presence of phenyl and carboxyl groups. These outcomes revealed the plan comprising of functionalized BTZ derivatives as enzyme modulators. In future work, similar results must be obtained through experiments along with the need for the development of better compounds for use in biocatalysis, environmental applications, and pharmaceuticals. This work lays a basis for the development of other DHP-targeting strategies employing derivatives of BTZ.