Fluorescence Quenching of Hen Egg Lysozyme and Bovine Serum Albumin by Azobenzene Polymer at Different pH

2014 ◽  
Vol 43 (9) ◽  
pp. 1499-1501
Author(s):  
Guoxiang Han ◽  
Ning Feng ◽  
Guojie Wang
1998 ◽  
Vol 95 (18) ◽  
pp. 10361-10366 ◽  
Author(s):  
C. V. Kumar ◽  
A. Buranaprapuk ◽  
G. J. Opiteck ◽  
M. B. Moyer ◽  
S. Jockusch ◽  
...  

Luminescence ◽  
2009 ◽  
pp. n/a-n/a ◽  
Author(s):  
U. S. Mote ◽  
S. L. Bhattar ◽  
S. R. Patil ◽  
G. B. Kolekar

2012 ◽  
Vol 135 (4) ◽  
pp. 2418-2424 ◽  
Author(s):  
Mihaela Skrt ◽  
Evgen Benedik ◽  
Črtomir Podlipnik ◽  
Nataša Poklar Ulrih

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


2008 ◽  
Vol 18 (3-4) ◽  
pp. 671-678 ◽  
Author(s):  
J. B. Xiao ◽  
X. Q. Chen ◽  
X. Y. Jiang ◽  
M. Hilczer ◽  
M. Tachiya

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