Study on the interaction characteristics of dexamethasone sodium phosphate with bovine serum albumin by spectroscopic technique

The interaction of dexamethasone sodium phosphate (DEX-P) with bovine serum albumin (BSA) was studied by fluorescence quenching in combination with UV-Vis spectroscopic method under near physiological conditions.

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In vitro Interactions of Secnidazole and Its Iron (II), Copper (II) Complexes with Bovine Serum Albumin by Fluorescence Quenching Method

Bangladesh Pharmaceutical Journal ◽

10.3329/bpj.v23i1.45313 ◽

2020 ◽

Vol 23 (1) ◽

pp. 1-9

Author(s):

Md Jamal Hossain ◽

Md Zakir Sultan ◽

Mohammad A Rashid ◽

Md Ruhul Kuddus

Keyword(s):

Bovine Serum Albumin ◽

Transition Metal ◽

Fluorescence Quenching ◽

Serum Albumin ◽

Metal Complexes ◽

Transition Metal Complexes ◽

Bovine Serum ◽

Spectroscopic Method ◽

Van Der Waals Interactions

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

Journal of Pharmaceutical Research International ◽

10.9734/jpri/2019/v30i630286 ◽

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.

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

Advanced Materials Research ◽

10.4028/www.scientific.net/amr.726-731.199 ◽

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.

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