Study of the interaction between fluoxetine hydrochloride and bovine serum albumin in the imitated physiological conditions by multi-spectroscopic methods

Fluorescence and UV spectroscopic techniques were used to investigate the interaction of Paeonolum, one of the major bioactive components isolated from the bark of peony plant, with bovine serum albumin (BSA). Results obtained reveal that a binding interaction occurs between paeonolum and BSA under physiological conditions, and the interaction can quench the fluorescence of BSA originating from the complex formation between paeonolum and BSA. In addition, according to the thermodynamics parameters of this interaction process, it appears that this binding interaction is mainly hydrophobic in nature.

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Interactions of linagliptin, rabeprazole sodium, and their formed complex with bovine serum albumin: Computational docking and fluorescence spectroscopic methods

Analytical Science Advances ◽

10.1002/ansa.202000153 ◽

2021 ◽

Author(s):

Md. Jamal Hossain ◽

Md. Zakir Sultan ◽

Mohammad A. Rashid ◽

Md. Ruhul Kuddus

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Spectroscopic Methods ◽

Computational Docking ◽

Rabeprazole Sodium

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Exploring the interactions of acenaphthene with bovine serum albumin: spectroscopic methods, molecular modeling and chemometric approaches

Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy ◽

10.1016/j.saa.2021.120164 ◽

2021 ◽

pp. 120164

Author(s):

Fatemeh Rostamnezhad ◽

Mohammad Hossein Fatemi

Keyword(s):

Molecular Modeling ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Spectroscopic Methods

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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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