Interaction of Potassium Mono and Di Phosphates with Bovine Serum Albumin Studied by Fluorescence Quenching Method

2010 ◽  
Vol 21 (2) ◽  
pp. 687-692 ◽  
Author(s):  
S. Bakkialakshmi ◽  
B. Shanthi ◽  
D. Chandrakala
Author(s):  
Kanij Nahar Deepa ◽  
Sabia Nawsheen ◽  
Md. Abu Sufian ◽  
S. M. Ashraful Islam

Background: The significant study was made to investigate the interaction of an antidiabetic drug, glimepiride with bovine serum albumin (BSA) by fluorescence quenching method in two different temperatures (298K and 308K). Methods: The study was carried out through fluorescence spectroscopic analysis. Stern-Volmer equation determined the fluorescence quenching constant. The various thermodynamic parameters such as free energy (ΔG), enthalpy (ΔH), and entropy (ΔS) was found out by Van’t Hoff equation. Results: The data revealed that glimepiride interact with BSA and both tryptophan and tyrosine residues of BSA are responsible for interactions with glimepiride. BSA undergo static quenching in presence of glimepiride, a quencher. The hydrophobic forces participated in chief roles for BSA-glimepiride complexation and this was indicated by the values of thermodynamic parameters. The binding number (n) obtained was ≈1 pointed out that glimepiride and BSA has bound with 1:1 ratio. Conclusions: Through fluorescence spectroscopic technique we revealed the nature of interaction of glimepiride with BSA, quenching mechanism for the interaction and associated thermodynamic parameters.


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


RSC Advances ◽  
2014 ◽  
Vol 4 (110) ◽  
pp. 64559-64564 ◽  
Author(s):  
Jafar Ezzati Nazhad Dolatabadi ◽  
Vahid Panahi-Azar ◽  
Abolfazl Barzegar ◽  
Ali Akbar Jamali ◽  
Fahimeh Kheirdoosh ◽  
...  

For the first time, PG interaction with HSA using fluorescence quenching method, circular dichroism spectroscopy and molecular modeling was investigated.


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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