Interaction Between Progesterone and Bovine Serum Albumin by Fluorescence Spectrum and Molecular Docking

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.

Download Full-text

Probing the behavior of bovine serum albumin upon binding to atenolol: insights from spectroscopic and molecular docking approaches

Journal of Biomolecular Structure and Dynamics ◽

10.1080/07391102.2017.1311805 ◽

2017 ◽

Vol 36 (5) ◽

pp. 1095-1107 ◽

Cited By ~ 14

Author(s):

Tuo-Ying Jiang ◽

Kai-Li Zhou ◽

Yan-Yue Lou ◽

Dong-qi Pan ◽

Jie-Hua Shi

Keyword(s):

Molecular Docking ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum

Download Full-text

Study of the Interactions of Bovine Serum Albumin with the New Anti-Inflammatory Agent 4-(1,3-Dioxo-1,3-dihydro-2H-isoindol-2-yl)-N′-[(4-ethoxy-phenyl)methylidene]benzohydrazide Using a Multi-Spectroscopic Approach and Molecular Docking

Molecules ◽

10.3390/molecules22081258 ◽

2017 ◽

Vol 22 (8) ◽

pp. 1258 ◽

Cited By ~ 25

Author(s):

Tanveer Wani ◽

Ahmed Bakheit ◽

Abdul-Rahman Al-Majed ◽

Mashooq Bhat ◽

Seema Zargar

Keyword(s):

Molecular Docking ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Inflammatory Agent ◽

Anti Inflammatory

Download Full-text

Study of Interaction Between Bovine Serum Albumin and Dolutegravir Intermediate: Fluorescence and Molecular Docking Analysis

Biointerface Research in Applied Chemistry ◽

10.33263/briac115.1310213110 ◽

2021 ◽

Vol 11 (5) ◽

pp. 13102-13110

Keyword(s):

Molecular Docking ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Binding Pocket ◽

Docking Analysis ◽

Free Binding Energy ◽

Steady State Fluorescence Spectroscopy ◽

Incremental Addition ◽

Molecular Docking Analysis

Novel (4R,12aS)-7-methoxy-4-methyl-6,8-dioxo-3,4,6,8,12,12a-hexahydro-2H-pyrido-[1',2':-4,5]-pyrazino[2,1-b][1,3]oxazine-9-carboxylic acid (L) was synthesized and characterised. The interaction between bovine serum albumin (BSA) with L was scrutinized by steady-state fluorescence spectroscopy, fluorescence anisotropy, fluorescence lifetime, and molecular docking methods. The fluorescence titration experiments of BSA resulted in fluorescence quenching with the incremental addition of L. The conformational binding of L to BSA has been investigated by molecular docking analysis. The molecular probe's best conformation showed the affinity as free binding energy release of -7.93 Kcal/mol. The docking analysis confirms that ligand binds in the near vicinity of TRP-213 in the binding pocket of subdomain IIA.

Download Full-text