NDLI: Thermodynamics, Conformation and Active Sites of the Binding of Zn–Nd Hetero-bimetallic Schiff Base to Bovine Serum Albumin

Content Provider	Springer Nature Link
Author	Xiao, Qi Huang, Shan Liu, Yi Tian, Fang fang Zhu, Jun cheng
Copyright Year	2008
Abstract	The interactions between N,N′-di(2-hydroxy-3-methyoxy-phenyl-1-methylene)-o-phenyldiamine-mone Zn(II), Nd(III) nitrate (2LZnNd) and bovine serum albumin (BSA) was investigated by various spectroscopic techniques under physiological conditions. It was proved that the fluorescence quenching of BSA by 2LZnNb was a result of the formation of a non-fluorescent complex with the binding constants of 3.15 × 10$^{5}$; 2.72 × 10$^{5}$ and 2.44 × 10$^{5}$ M$^{–1}$ at 298 K, 304 K and 310 K, respectively. A marked increase in the fluorescence anisotropy in the proteinous environments indicates that BSA introduces motional restriction on the drug molecule. The corresponding thermodynamics parameters ΔH and ΔS were calculated to be –16.36 kJ mol$^{–1}$ and 43.48 J mol$^{–1}$ K$^{–1}$ via van’t Hoff equation. Moreover, the competitive probes experiment revealed that the binding location of 2LZnNb to BSA is in the hydrophobic pocket of site II. The effect of 2LZnNb on the conformation of BSA has been analyzed by means of CD spectrum and three-dimensional fluorescence spectra. The results indicate that the conformation of BSA molecules was changed in the presence of 2LZnNb Schiff base.
Starting Page	317
Ending Page	326
Page Count	10
File Format	PDF
ISSN	10530509
Journal	Journal of Fluorescence
Volume Number	19
Issue Number	2
e-ISSN	15734994
Language	English
Publisher	Springer US
Publisher Date	2008-10-21
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Bovine serum albumin Circular dichroism Competitive probe Schiff base Thermodynamic parameters Analytical Chemistry Biochemistry Biotechnology Biophysics/Biomedical Physics Biomedicine general
Content Type	Text
Resource Type	Article
Subject	Sociology and Political Science Spectroscopy Law Biochemistry Clinical Biochemistry Clinical Psychology

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