Open AccessIn vitro Interactions of Secnidazole and Its Iron (II), Copper (II) Complexes with Bovine Serum Albumin by Fluorescence Quenching Method
Author(s) -
Md. Jamal Hossain,
Zakir Sultan,
Mohammad A. Rashid,
Ruhul Kuddus
Publication year - 2020
Publication title -
bangladesh pharmaceutical journal
Language(s) - English
Resource type - Journals
eISSN - 2408-8463
pISSN - 0301-4606
DOI - 10.3329/bpj.v23i1.45313
Subject(s) - chemistry , bovine serum albumin , van der waals force , quenching (fluorescence) , enthalpy , fluorescence , gibbs free energy , binding constant , metal , hydrogen bond , copper , crystallography , nuclear chemistry , chromatography , binding site , organic chemistry , molecule , biochemistry , thermodynamics , physics , quantum mechanics
The current study was designed to investigate the interactions of an antimicrobial drug secnidazole and its two transition metal complexes with bovine serum albumin (BSA). The interactions of secnidazole and its both transition metal complexes were confirmed by the extingushing of fluorescence intensity of the protein. The fluorescence quenching of BSA by the drug and its both metal complexes showed a static quenching process and the reactions followed exothermic mechanism. The fluorescence spectroscopic method was utilized to evaluate the thermodynamic parameters like change of enthalpy (ΔH), entropy (ΔS) and Gibb’s free energy (ΔG) which indicated the bindings of the antimicrobial agent and its both metal chelates were hydrogen bonding and van der Waals interactions. The binding constant and the number of binding sites were also measured by double log plot that indicated the drug or its metal complexes bound with BSA at 1:1 ratio.
Bangladesh Pharmaceutical Journal 23(1): 1-9, 2020