Luminescence, circular dichroism and in silico studies of binding interaction of synthesized naphthylchalcone derivatives with bovine serum albumin

Abstract

Chalcones possess various biological properties, for example, antimicrobial, anti-inflammatory, analgesic, antimalarial, anticancer, antiprotozoal and antitubercular activity. In this study, naphthylchalcone derivatives were synthesized and characterized using H NMR C NMR, Fourier transform infrared and mass techniques. Yields for all derivatives were found to be >90%. Protein-drug interactions influence the absorption, distribution, metabolism and excretion (ADME) properties of a drug. Therefore, to establish whether the synthesized naphthylchalcone derivatives can be used as drugs, their binding interaction toward a serum protein (bovine serum albumin) was investigated using fluorescence, circular dichroism and molecular docking techniques under physiological conditions. Fluorescence quenching of the protein in the presence of naphthylchalcone derivatives, and other derived parameters such as association constants, number of binding sites and static quenching involving confirmed non-covalent binding interactions in the protein-ligand complex were observed. Circular dichroism clearly showed changes in the secondary structure of the protein in the presence of naphthylchalcones, indicating binding between the derivatives and the serum protein. Molecular modelling further confirmed the binding mode of naphthylchalcone derivatives in bovine serum albumin. A site-specific molecular docking study of naphthylchalcone derivatives with serum albumin showed that binding took place primarily in the aromatic low helix and then in subdomain II. The dominance of hydrophobic, hydrophilic and hydrogen bonding was clearly visible and was responsible for stabilization of the complex.

Synthesis, DFT studies, molecular docking, antimicrobial screening and UV fluorescence studies on ct-DNA for novel Schiff bases of 2-(1-aminobenzyl) benzimidazole

“…The molecular docking technique helps in understanding non-covalent drug-DNA interactions of small molecules into the targeted region of DNA for rational drug design and discovery. The minor groove of DNA is preferred over major one due to lesser steric hindrance, electrostatic factors and its narrow shape [35, 36, 37, 38, 39, 40].…”

Study on the interaction of kojic acid with tyrosinase by spectroscopic methods

“…To explain the probable mechanism for quenching, the fluorescence quenching at three temperatures was carried out, including 288, 298, and 310 Kelvin ( Figure 3A). The Stern -Volmer plot displayed a good linear relationship under the concentration range, suggesting that only a single quenching type occurred [7,12,19]. The k q values at different temperatures appeared much larger than the maximum diffusion collision quenching rate constant (2×10 10 M -1 s -1 ) ( Table 1) [7,9,21].…”

Elucidation on inhibition and binding mechanism of bovine liver catalase by nifedipine: multispectroscopic analysis and computer simulation methods

“…The pharmacological properties of ligands as drugs in organisms are strongly related to their interactions with biological proteins. [29][30][31][32] As a common enzyme in aerobic organism, catalase can rapidly decompose H 2 O 2 into H 2 O and O 2 . H 2 O 2 can play important roles physiologically and pathologically either as a beneficial signalling agent or a toxic hazard, and which one depends on its concentration in vivo.…”