Studies on interaction of vanadium metal complexes with bovine serum albumin - Fluoremetric and UV–visible spectrophotometric studies

2019 ◽  
Vol 20 ◽  
pp. 100203 ◽  
Author(s):  
Vani Kondaparthy ◽  
Ayub Shaik ◽  
Kunduru Bharathi Reddy ◽  
Deva Das Manwal
2020 ◽  
Vol 23 (1) ◽  
pp. 1-9
Author(s):  
Md Jamal Hossain ◽  
Md Zakir Sultan ◽  
Mohammad A Rashid ◽  
Md Ruhul Kuddus

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


2016 ◽  
Vol 128 (11) ◽  
pp. 1783-1788 ◽  
Author(s):  
GUIFANG YAN ◽  
YUFENG HE ◽  
GANG LI ◽  
YUBING XIONG ◽  
PENGFEI SONG ◽  
...  

2007 ◽  
Vol 18 (11) ◽  
pp. 1416-1418 ◽  
Author(s):  
Rong Min Wang ◽  
Juan Juan Mao ◽  
Jing Feng Song ◽  
Cai Xia Huo ◽  
Yu Feng He

RSC Advances ◽  
2018 ◽  
Vol 8 (71) ◽  
pp. 40720-40730 ◽  
Author(s):  
Jie Tang ◽  
Pengfei Yao ◽  
Lina Wang ◽  
Hedong Bian ◽  
Meiyi Luo ◽  
...  

Artificial metalloenzymes have been prepared by non-covalent insertion of transition metal Schiff-base complexes into bovine serum albumin as the host protein and were characterized by UV-visible spectroscopy, ESI-TOF mass spectrometry and molecular docking studies.


2014 ◽  
Vol 87 (4) ◽  
pp. 215-219 ◽  
Author(s):  
Tamara Topală ◽  
Andreea Bodoki ◽  
Luminiţa Oprean ◽  
Radu Oprean

The continuous search for new molecules with therapeutic abilities has led to the synthesis and characterization of a large number of metal complexes, proven to exhibit potential as pharmacological agents through their antibacterial, antiviral, antifungal and antineoplastic properties. As serum albumins play a key role in drug pharmacokinetics and pharmacodynamics, the study of coordination compounds affinity towards this class of proteins, as well as understanding the mechanism through which they interact is crucial. The aim of this review is to focus on the structure and biological functions of bovine serum albumin, the design of metal complexes that are able to bind to the biomolecule, as well as the experimental techniques employed in the study and evaluation of these interactions. Keywords: drug-protein interaction, coordination complex, fluorescence spectroscopy, UV-Vis absorption spectroscopy.


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