scholarly journals Combined molecular docking, homology modeling and DFT method for the modification of bovine serum albumin (BSA) to improve fluorescence spectroscopy for phthalate acid esters chelated with BSA

BIOCELL ◽  
2020 ◽  
Vol 44 (2) ◽  
pp. 247-255
Author(s):  
MINGHAO LI ◽  
YOULI QIU ◽  
WENHUI ZHANG ◽  
RUIHAO SUN ◽  
MEIJIN DU ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Homology Modeling ◽  
Bovine Serum ◽  
Dft Method ◽  
Acid Esters ◽  
Phthalate Acid Esters

scholarly journals Spectroscopic, voltammetry and molecular docking study of binding interaction of antipsychotic drug with bovine serum albumin

2016 ◽  
Vol 6 (2) ◽  
pp. 155 ◽  
Author(s):  
Mallappa Mahanthappa ◽  
Babu Giriya Gowda ◽  
Jayant I. Gowda ◽  
Raghavendran Rengaswamy
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Free Energy ◽  
Acetate Buffer ◽  
Acetate Buffer Solution ◽  
Binding Interaction ◽  
Vis Spectroscopy

<p class="PaperAbstract"><span lang="EN-GB">The interaction between perazine dimaleate (PDM) and bovine serum albumin (BSA) was investigated by voltammetry, fluorescence spectroscopy, UV–vis spectroscopy, molecular docking and viscometric methods. The study was carried out in acetate buffer solution of pH 7.2, which was prepared by using 0.1 M sodium acetate and adjusting pH using 0.1 M hydrochloric acid. The voltammetric study of PDM shows a pair of well redox peaks at 0.538 and 0.471 V (versus SCE) on a GCE in acetate buffer of pH 7.2 at <br /> 50 mV s<sup>-1</sup>. After the addition of BSA into the PDM solution, the redox peak currents decreased gradually, and peak potentials shifted towards negative direction. The results of voltammetry, fluorescence quenching and UV–vis absorption spectra experiments indicated the formation BSA–PDM complex. The binding parameters like binding con­stant and binding free energy were determined from voltammetric data. The binding constant and binding energy was also determined from UV–vis and fluorescence spectroscopy with a value quite close to that obtained from CV.</span></p>

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

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.

scholarly journals Spectroscopic, thermodynamic and molecular docking studies of bovine serum albumin interaction with ascorbyl palmitate food additive

Bioimpacts ◽  
2017 ◽  
Vol 7 (4) ◽  
pp. 241-246 ◽  
Author(s):  
Yousef Sohrabi ◽  
Vahid Panahi-Azar ◽  
Abolfazl Barzegar ◽  
Jafar Ezzati Nazhad Dolatabadi ◽  
Parvin Dehghan
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Ascorbyl Palmitate ◽  
Docking Studies ◽  
Food Additive ◽  
Molecular Docking Studies
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