Title
Insight into the interaction of benzothiazole tethered triazole analogues with human serum albumin: Spectroscopy and molecular docking approaches
Author
Priyanka Yadav, Jitendra Kumar Yadav, Arvind Kumar Dixit, Alka Agarwal, Satish Kumar Awasthi
Year
2019
Journal
Luminescence
Abstract
The interaction of four benzothiazole tethered triazole analogues (MS43, MS70, MS71, and MS78) with human serum albumin (HSA) was investigated using various spectroscopic techniques (ultraviolet–visible (UV–vis) light absorption, fluorescence, circular dichroism (CD), molecular docking and density functional theory (DFT) studies). Fluorescence quenching constants (~1012) revealed a static mode of quenching and binding constants (Kb ~104) indicating the strong affinity of these analogues for HSA. Further alteration in the secondary structure of HSA in the presence of these analogues was also confirmed by far UV–CD spectroscopy. The intensity loss in CD studied at 222 nm indicated an increase in random coil/β‐sheet conformations in the protein. Binding energy values (MS71 (−9.3 kcal mol−1), MS78 (−8.02 kcal mol−1), MS70 (−7.16 kcal mol−1) and MS43 (−6.81 kcal mol−1)) obtained from molecular docking revealed binding of these analogues with HSA. Molecular docking and DFT studies validated the experimental results, as these four analogues bind with HSA at site II through hydrogen bonding and hydrophobic interactions.
Instrument
V-670, J-810
Keywords
Absorption, Protein structure, Ligand binding, Circular dichroism, Secondary structure, Biochemistry