scholarly journals Bovine serum albumin interactions with metal complexes

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.

2019 ◽  
Vol 55 (3) ◽  
pp. 318-325
Author(s):  
Xiaofang Wang ◽  
Luyi Zou ◽  
Chenyu Mi ◽  
Hongyan Yu ◽  
Mengxue Dong ◽  
...  

2019 ◽  
Vol 278 ◽  
pp. 203-207 ◽  
Author(s):  
Bo-Bae Koh ◽  
Eun-Jung Lee ◽  
Karna Ramachandraiah ◽  
Geun-Pyo Hong

1986 ◽  
Vol 49 (4) ◽  
pp. 267-271 ◽  
Author(s):  
RU-DONG WEI ◽  
WILLIAM BISCHOFF ◽  
FUN SUN CHU

Antibody raised against T-2 toxin cross-reacted poorly with 3′-OH-T-2 toxin. A new immunogen was prepared by conjugation of hemisuccinate (HS) of 3′-OH-T-2 toxin to bovine serum albumin (BSA). Antibodies against 3′-OH-T-2 toxin were demonstrated by a radioimmunoassay 10 wk after immunization of rabbits with this new immunogen using tritiated 3′-OH-T-2 toxin as the testing ligand. Highest titers (1:6,000) were obtained 17 wk after immunization and two booster injections. The antibodies had good cross-reactivity with T-2 toxin, acetyl-T-2 toxin and 3′-OH-acetyl-T-2 toxin. The relative cross-reactivity of this antibody with 3′-OH-T-2, acetyl-T-2, T-2, 3′-OHacetyl-T-2, 3′-OH-T-2-HS, T-2 isomer, HT-2 and 3′-OH-HT-2 was 1, 3, 4, 5, 15, 30, 45 and 175, respectively. No crossreaction was found when 3′-OH-T-2 triol, T-2-triol, T-2-tetraol, DAS and DON at a concentration of 1 μg per assay was tested. The detection limit for 3′-OH-T-2 toxin by the RIA was about 0.1 ng per assay.


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


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