scholarly journals Spectroscopic and molecular docking elucidation to binding characteristics of bovine serum albumin with bupropion an aminoketone-medication for nicotine addiction

2019 ◽  
Vol 10 (2) ◽  
pp. 146-155
Author(s):  
Manjushree Makegowda ◽  
Revanasiddappa Hosakere Doddarevanna
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Circulatory System ◽  
Biologically Active ◽  
Binding Characteristics ◽  
Active Metal ◽  
Ft Ir ◽  
Binding Forces

One of the highly soluble protein presents in circulatory system of bovine body is bovine serum albumin (BSA). Bupropion hydrochloride (BRN) served to treat prime smoking cessation and disorder due to depressive. BRN binding to BSA was studied by molecular docking and lots of spectroscopic (UV-vis, emission, synchronous, 3D fluorescence, CD and FT-IR) methods at pH = 7.40. Static quenching with strong binding was obtained for BSA-BRN system by forming complex. Secondary structures, conformations and microenvironments of BSA were altered after BRN interaction. Distance between BRN and BSA was also achieved. Biologically active metal ions (Cu2+, Ca2+, Mg2+, Fe2+ and Zn2+) were also influenced on the BSA-BRN complex. Bonds of hydrogen and Van der Waals were major binding forces to stabilize BSA-BRN complex at site I (IIA) of BSA. Hence, binding of BRN to transport protein (BSA) is of prominent importance and these findings could be helpful for BRN pharmacology and potential clinical research.

scholarly journals A Diversified Spectrometric and Molecular Docking Technique to Biophysical Study of Interaction between Bovine Serum Albumin and Sodium Salt of Risedronic Acid, a Bisphosphonate for Skeletal Disorders

2018 ◽  
Vol 2018 ◽  
pp. 1-13 ◽  
Author(s):  
M. Manjushree ◽  
Hosakere D. Revanasiddappa
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Sodium Salt ◽  
Bovine Serum ◽  
Biologically Active ◽  
Risedronic Acid ◽  
Binding Interaction ◽  
Vis Spectroscopy ◽  
Ft Ir

The binding interaction between bovine serum albumin (BSA) and sodium salt of risedronic acid (RSN) was studied by using the FT-IR (Fourier transform infrared), UV-Vis (ultraviolet–visible), fluorescence (emission and synchronous), CD (circular dichroism) spectrometric, and computational (molecular docking) techniques at 289, 297, and 305 K temperatures with physiological buffer of pH 7.40. The conformational and secondary structural changes observed for BSA from CD spectra and by curve fitting procedure were applied to Fourier self-deconvolution in FT-IR spectra. The formation of a BSA-RSN complex was confirmed from UV-Vis spectroscopy. The static type of quenching shown for RSN to BSA was verified from Stern–Volmer and modified Stern–Volmer equations. The binding constant of order 105 was obtained to be confirming that there exists a strong binding interaction between BSA and RSN. Synchronous fluorescence shows that the microenvironment of tryptophan was altered, not tyrosine of BSA; in addition to this, the distance between tryptophan of BSA and RSN was found out from Forster’s theory of nonradiation energy transfer. The interaction between BSA and RSN mainly occurred as a result of hydrogen bonds and van der Waals forces, the process is exothermic and spontaneous, and it was achieved through van ’t Hoff equation. This interaction was affected by the presence of biologically active Fe2+, Ni2+, Ca2+, Mg2+, and Cd2+ ions and was also studied. The subdomain IIIA of BSA involved with RSN interaction was authenticated from molecular docking analysis.

scholarly journals Design and Synthesis of Novel 1,3-Thiazole and 2-Hydrazinyl-1,3-Thiazole Derivatives as Anti-Candida Agents: In Vitro Antifungal Screening, Molecular Docking Study, and Spectroscopic Investigation of their Binding Interaction with Bovine Serum Albumin

Molecules ◽  
2019 ◽  
Vol 24 (19) ◽  
pp. 3435 ◽  
Author(s):  
Andreea-Iulia Pricopie ◽  
Ioana Ionuț ◽  
Gabriel Marc ◽  
Anca-Maria Arseniu ◽  
Laurian Vlase ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Rapid Development ◽  
Biologically Active ◽  
Thiazole Derivatives ◽  
Binding Interaction ◽  
Reference Drug

In the context of there being a limited number of clinically approved drugs for the treatment of Candida sp.-based infections, along with the rapid development of resistance to the existing antifungals, two novel series of 4-phenyl-1,3-thiazole and 2-hydrazinyl-4-phenyl-1,3-thiazole derivatives were synthesized and tested in vitro for their anti-Candida potential. Two compounds (7a and 7e) showed promising inhibitory activity against the pathogenic C. albicans strain, exhibiting substantially lower MIC values (7.81 μg/mL and 3.9 μg/mL, respectively) as compared with the reference drug fluconazole (15.62 μg/mL). Their anti-Candida activity is also supported by molecular docking studies, using the fungal lanosterol C14α-demethylase as the target enzyme. The interaction of the most biologically active synthesized compound 7e with bovine serum albumin was investigated through fluorescence spectroscopy, and the obtained data suggested that this molecule might efficiently bind carrier proteins in vivo in order to reach the target site.

scholarly journals Molecular Docking and Extended Spectroscopy to Binding Characterizations: Etoposide a Glycoside of Podophyllotoxin with Bovine Serum Albumin

2021 ◽  
Vol 12 (1) ◽  
pp. 264-278
Keyword(s):  
Drug Delivery ◽  
Energy Transfer ◽  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Discovery Process ◽  
Binding Interaction ◽  
Bsa Binding ◽  
Ft Ir

A significant soluble protein, specifically bovine serum albumin (BSA) plays an efficient role in drug delivery, and etoposide (ETS) is used to cure various cancers. Binding interaction between ETS and BSA examined by 3D, emission, synchronous fluorescence’s, UV–vis, FT–IR, and CD spectroscopy’s in the association of computational at pH 7.40 with 293, 301 and 309 K. Formed complex between ETS and BSA dominates van der Waals and bonding of hydrogen’s at sub-domain IIIA. Strong binding of ETS-BSA leads to altering BSA’s structural and conformations statically. Energy transfer reveals ETS-BSA distance. Apart from this, ETS-BSA binding is affected by Mg2+, Cu2+, Fe2+, Ca2+, and Co2+ ions. This study may help in the drug development and discovery process.

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.

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