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Spectroscopic evaluation of Zn (II) complexes with drug analogues: Interactions with BSA and the pH effect on the drug-Zn (II) system.

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Title: Spectroscopic evaluation of Zn (II) complexes with drug analogues: Interactions with BSA and the pH effect on the drug-Zn (II) system.
Authors: Vlasiou, Manolis C.1 (AUTHOR) vlasiou.m@unic.ac.cy, Pafiti, Kyriaki S.1 (AUTHOR)
Source: Spectrochimica Acta Part A: Molecular & Biomolecular Spectroscopy. Nov2020, Vol. 241, pN.PAG-N.PAG. 1p.
Subjects: pH effect, Acetamide, Zinc ions, Zinc compounds, Carrier proteins, Amino acid residues, Fluorescence spectroscopy, Drug interactions
Abstract: Using UV–Vis, FT-IR, fluorescence spectroscopy and protein-ligand docking, the interactions between the zinc complexes with drug analogues and bovine serum albumin were investigated. In addition, considering the ubiquitous presence of zinc ions in the human system, we studied the interactions between this ion with hymecromone, dihydropyridine analogue, and acetamide, as well as the pH influence on these systems. The complexes were synthesized by interaction between the ligands and the Zn (II) ion in a 2:1 M ratio. Elemental analysis, FT-IR, and UV–Vis spectroscopy studies investigated the structure of the synthesized complexes. Fluorescence spectroscopy, UV–Vis, molecular docking and molecular dynamics were used to study the interactions of the Zn complexes with the BSA. The drug-Zn (II) system's pH effect was investigated using UV–Vis spectroscopy. After the complexation with the zinc, the drug molecules exhibited higher apparent binding affinity to BSA. BSA's fluorescence efficiency by the drug analogues was enhanced. In addition, molecular modelling was used to classify the residue of amino acids in the BSA playing key roles in this binding interaction. An increase in pH appears to contribute to alkaline hydrolysis of the Zn (II) molecules. Unlabelled Image • Zinc metal ions contributes to different binding affinities of drugs on transport proteins. • Drug analogues can be vehicles for Zn and allies to its redox potential. • Zinc-drug complexes could be unstable to light alkaline conditions. [ABSTRACT FROM AUTHOR]
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Database: Engineering Source
Description
Abstract:Using UV–Vis, FT-IR, fluorescence spectroscopy and protein-ligand docking, the interactions between the zinc complexes with drug analogues and bovine serum albumin were investigated. In addition, considering the ubiquitous presence of zinc ions in the human system, we studied the interactions between this ion with hymecromone, dihydropyridine analogue, and acetamide, as well as the pH influence on these systems. The complexes were synthesized by interaction between the ligands and the Zn (II) ion in a 2:1 M ratio. Elemental analysis, FT-IR, and UV–Vis spectroscopy studies investigated the structure of the synthesized complexes. Fluorescence spectroscopy, UV–Vis, molecular docking and molecular dynamics were used to study the interactions of the Zn complexes with the BSA. The drug-Zn (II) system's pH effect was investigated using UV–Vis spectroscopy. After the complexation with the zinc, the drug molecules exhibited higher apparent binding affinity to BSA. BSA's fluorescence efficiency by the drug analogues was enhanced. In addition, molecular modelling was used to classify the residue of amino acids in the BSA playing key roles in this binding interaction. An increase in pH appears to contribute to alkaline hydrolysis of the Zn (II) molecules. Unlabelled Image • Zinc metal ions contributes to different binding affinities of drugs on transport proteins. • Drug analogues can be vehicles for Zn and allies to its redox potential. • Zinc-drug complexes could be unstable to light alkaline conditions. [ABSTRACT FROM AUTHOR]
ISSN:13861425
DOI:10.1016/j.saa.2020.118641