scholarly journals Spectroscopic Studies of the Interaction between Metformin Hydrochloride and Bovine Serum Albumin

2012 ◽  
Vol 11 (1) ◽  
pp. 45-49 ◽  
Author(s):  
Ahmad Tanwir ◽  
Rahat Jahan ◽  
Mohiuddin Abdul Quadir ◽  
Mohammad A Kaisar ◽  
Md Khalid Hossain
Keyword(s):  
Hydrogen Bond ◽  
Bovine Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Studies ◽  
Metformin Hydrochloride ◽  
Tryptophan Residue ◽  
Different Temperatures ◽  
Hoff Equation

The affinity of a drug to serum albumin has influence on the pharmacokinetics of a drug. In the present study, the mutual interaction of metformin hydrochloride (MET) with bovine serum albumin (BSA) was investigated using fluorescence spectroscopy under different conditions. It was observed that the fluorescence  quenching of BSA by metformin hydrochloride is a result of the formation of metformin hydrochloride- BSA complex with probable involvement of tryptophan residue. Fluorescence quenching constants were determined using  the Stern- Volmer equation and Van’t Hoff equation to provide a measure of the thermodynamic parameters ?G, ?H, and ?S at different temperatures indicating that the hydrogen bond and the hydrophobic forces play a major role for metformin hydrochloride- BSA association. DOI: http://dx.doi.org/10.3329/dujps.v11i1.12486 Dhaka Univ. J. Pharm. Sci. 11(1): 45-49, 2012 (June)

scholarly journals In-vitro Fluorescence Spectroscopic Analysis of the Interaction of Glimepiride with Bovine Serum Albumin (BSA)

2019 ◽  
pp. 1-8
Author(s):  
Kanij Nahar Deepa ◽  
Sabia Nawsheen ◽  
Md. Abu Sufian ◽  
S. M. Ashraful Islam
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Thermodynamic Parameters ◽  
Bovine Serum ◽  
Spectroscopic Analysis ◽  
Spectroscopic Technique ◽  
Different Temperatures ◽  
Quenching Method

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.

BOVINE SERUM ALBUMIN FLUORESCENCE QUENCHING BY TANNIC ACID IN DIMETHYLSULFOXIDE CONTAINING SOLUTIONS

2020 ◽  
Vol 54 (2 (252)) ◽  
pp. 99-104
Author(s):  
K.R. Grigoryan ◽  
H.A. Shilajyan ◽  
V.A. Hovhannisyan
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Tannic Acid ◽  
Bovine Serum ◽  
Structural Changes ◽  
Different Temperatures ◽  
Fluorescence Quenching Mechanism ◽  
Bimolecular Quenching ◽  
Bsa Interaction

Bovine serum albumin (BSA) interaction with tannic acid (TA) has been studied in dimethylsulfoxide (DMSO) aqueous solutions at different temperatures (293 and 303 K). To find out the fluorescence quenching mechanism of BSA in the presence of TA, the fluorescence data were analyzed according to the modified Stern-Volmer equation based on the approach of the existence of a “sphere of action” (a type of apparent static quenching). The values of apparent static and bimolecular quenching constants were calculated. The effect of DMSO and temperature on BSA–TA interactions is explained on the basis of structural changes in the “sphere of action” of the fluorophore due to the possible inclusion of DMSO molecules in this sphere.

Spectroscopic Studies on Interaction of Friedelin with Bovine Serum Albumin

2012 ◽  
Vol 18 (2) ◽  
pp. 287
Author(s):  
Zhiwei LIN ◽  
Zhengfu TAI ◽  
Zhongmin WAN ◽  
Fei WANG ◽  
Ningfei LEI
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Studies

Spectroscopic Studies on the Binding of Bacteriophage Mequindox with Bovine Serum Albumin

2009 ◽  
Vol 27 (4) ◽  
pp. 681-686 ◽  
Author(s):  
Zhouhua ZENG ◽  
Yi LIU ◽  
Xianming HU ◽  
Zhenqiang XU ◽  
Kun ZENG
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Studies

Studies on the Interaction between Imidacloprid and Bovine Serum Albumin by Spectrometry

2013 ◽  
Vol 726-731 ◽  
pp. 199-203
Author(s):  
Rui Xin Guo ◽  
Zhi Liang Wang ◽  
Zhi Jun Hu ◽  
Guo Ling Li ◽  
Jian Qiu Chen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Fluorescence Spectrum ◽  
Bovine Serum ◽  
Synchronous Fluorescence ◽  
Binding Studies ◽  
Single Class ◽  
Physiological Conditions ◽  
Synchronous Fluorescence Spectrometry ◽  
Hoff Equation

The binding studies of imidacloprid to bovine serum albumin (BSA) were investigated by UV-Vis absorption spectrum, fluorescence spectrum and synchronous fluorescence spectrometry. Under the simulative physiological conditions, fluorescence data revealed the presence of a single class of binding site on BSA and the dynamic quenching constants () were 6.851×104 L.mol-1 and 5.813×104 L.mol-1 at 310 and 315 K, respectively, proving the mode of action of imidacloprid with BSA as a static quenching. In addition, according to the Vant Hoff equation, ΔGθ <0 showed="" the="" combination="" of="" imidacloprid="" and="" bsa="" was="" a="" spontaneous="" process="" h="" sup="">θ <0 and="" s="" sup="">θ> 0, indicated an electrostatic interaction process. At the same time, synchronous fluorescence spectrum of BSA could tell us whether the conformation of BSA was changed by imidacloprid.

Interaction between felodipine and bovine serum albumin: fluorescence quenching study

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

scholarly journals Physicochemical Peculiarities of Iodine-Dimethylsulfoxide-H2O Solutions and Effect on Ion Binding to Bovine Serum Albumin

2013 ◽  
Vol 2013 ◽  
pp. 1-5
Author(s):  
K. Grigoryan ◽  
H. Shilajyan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Entropy Change ◽  
Ion Binding ◽  
Fluorescence Energy Transfer ◽  
Iodide Ion ◽  
Different Temperatures ◽  
Fluorescence Energy

The interaction of iodine with bovine serum albumin (BSA) in dimethylsulfoxide (DMSO) aqueous solutions was studied by means of fluorescence and UV/Vis absorption spectroscopy methods. Physicochemical peculiarities of these solutions were revealed. The results showed that the tri-iodide ion formed in the 1DMSO : 2H2O solution caused the fluorescence quenching of BSA. The modified Stern-Volmer quenching constant and corresponding thermodynamic parameters, the free energy change (), enthalpy change (), and entropy change (), at different temperatures (293, 298, and 303 K) were calculated, which indicated that the hydrophobic and electrostatic interactions were the predominant operating forces. The binding locality distance r between BSA and tri-iodide ion at different temperatures was determined based on Förster nonradiation fluorescence energy transfer theory.

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