A study of the interaction between fluorescein sodium salt and bovine serum albumin by steady-state fluorescence

2009 ◽  
Vol 80 (3) ◽  
pp. 307-313 ◽  
Author(s):  
N BARBERO ◽  
E BARNI ◽  
C BAROLO ◽  
P QUAGLIOTTO ◽  
G VISCARDI ◽  
...  
Keyword(s):  
Steady State ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Sodium Salt ◽  
Bovine Serum ◽  
Fluorescein Sodium ◽  
Steady State Fluorescence ◽  
Fluorescein Sodium Salt

Exploration of interactions between decyl-β-d-glucopyranoside and bovine serum albumin in aqueous solution

RSC Advances ◽  
2016 ◽  
Vol 6 (24) ◽  
pp. 19700-19706 ◽  
Author(s):  
Gongke Wang ◽  
Huimin Hou ◽  
Ye Chen ◽  
Changling Yan ◽  
Guangyue Bai ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Surface Tension ◽  
Steady State ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Absorption Spectroscopy ◽  
Bovine Serum ◽  
Aqueous Media ◽  
Steady State Fluorescence

The interactions between decyl-β-d-glucopyranoside (DG) and bovine serum albumin (BSA), in aqueous media, were investigated through the use of surface tension, steady-state fluorescence, and UV-vis absorption spectroscopy measurements.

scholarly journals Molecular imprinting of bovine serum albumin and lysozyme within the matrix of polyampholyte hydrogels based on acrylamide, sodium salt of 2-acrylamido-2-methyl-1-propanesulfonic acid and (3-acrylamidopropyl)trimethyl ammonium chloride

2021 ◽  
pp. 4-11
Author(s):  
Alexey Shakhvorostov ◽  
Sarkyt Kudaibergenov
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Ammonium Chloride ◽  
Sodium Salt ◽  
Bovine Serum ◽  
In Situ Polymerization ◽  
Trimethyl Ammonium Chloride ◽  
Cationic Monomer ◽  
The Matrix ◽  
Adsorption Desorption

Molecularly-imprinted polyampholyte (MIP) hydrogels based on nonionic monomer – acrylamide (AAm), anionic monomer – sodium salt of 2-acrylamido-2-methyl-1-propanesulfonic acid (AMPS) and cationic monomer – (3-acrylamidopropyl)trimethyl ammonium chloride (APTAC) were obtained by immobilization of bovine serum albumin (BSA) and lysozyme in situ polymerization conditions. It was found that the best amphoteric hydrogel for sorption of BSA is APTAC-75H while for sorption of lysozyme is AMPS-75H. The sorption capacity of APTAC-75H and AMPS-75H with respect to BSA and lysozyme is 305.7 and 64.1-74.8 mg per 1 g of hydrogel respectively. Desorption of BSA and lysozyme from MIP template performed by aqueous solution of 1M NaCl is equal to 82-88%. Separation of BSA and lysozyme from their mixture was performed on MIP templates. The results of adsorption-desorption cycles of BSA on adjusted to BSA polyampholyte hydrogel APTAC-75H and of lysozyme on adjusted to lysozyme polyampholyte hydrogel AMPS-75H show that the mixture of BSA and lysozyme can be selectively separated with the help of MIP hydrogels.

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.

Sign in / Sign up

Export Citation Format

Share Document