Electrophoretic Analysis of Protein Interaction. II. Explanation of a Boundary Anomaly in the System Bovine Serum Albumin–Methyl Orange

1952 ◽  
Vol 56 (6) ◽  
pp. 717-722 ◽  
Author(s):  
J. Ross Colvin ◽  
D. R. Briggs
Keyword(s):  
Methyl Orange ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Interaction ◽  
Bovine Serum ◽  
Electrophoretic Analysis

scholarly journals Grafting Thin Layered Graphene Oxide onto the Surface of Nonwoven/PVDF-PAA Composite Membrane for Efficient Dye and Macromolecule Separations

Nanomaterials ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 792
Author(s):  
Febri Baskoro ◽  
Selvaraj Rajesh Kumar ◽  
Shingjiang Jessie Lue
Keyword(s):  
Graphene Oxide ◽  
Folic Acid ◽  
Methyl Orange ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Composite Membrane ◽  
Polyacrylic Acid ◽  
Bovine Serum ◽  
Polyvinylidene Fluoride ◽  
Oxide Composite

This study investigates the permeance and rejection efficiencies of different dyes (Rhodamine B and methyl orange), folic acid and a protein (bovine serum albumin) using graphene oxide composite membrane. The ultrathin separation layer of graphene oxide (thickness of 380 nm) was successfully deposited onto porous polyvinylidene fluoride-polyacrylic acid intermediate layer on nonwoven support layer using vacuum filtration. The graphene oxide addition in the composite membrane caused an increased hydrophilicity and negative surface charge than those of the membrane without graphene oxide. In the filtration process using a graphene oxide composite membrane, the permeance values of pure water, dyes, folic acid and bovine serum albumin molecules were more severely decreased (by two orders of magnitude) than those of the nonwoven/polyvinylidene fluoride-polyacrylic acid composite membrane. However, the rejection efficiency of the graphene oxide composite was significantly improved in cationic Rhodamine B (from 9% to 80.3%) and anionic methyl orange (from 28.3% to 86.6%) feed solutions. The folic acid and bovine serum albumin were nearly completely rejected from solutions using either nonwoven/polyvinylidene fluoride-polyacrylic acid or nonwoven/polyvinylidene fluoride-polyacrylic acid/graphene oxide composite membrane, but the latter possessed anti-fouling property against the protein molecules. The separation mechanism in nonwoven/polyvinylidene fluoride-polyacrylic acid membrane includes the Donnan exclusion effect (for smaller-than-pore-size solutes) and sieving mechanism (for larger solutes). The sieving mechanism governs the filtration behavior in the nonwoven/polyvinylidene fluoride-polyacrylic acid/graphene oxide composite membrane.

Binding characteristics of bovine serum albumin encapsulated in sol-gel glasses: An alternative for protein interaction studies

2008 ◽  
Vol 373 (2) ◽  
pp. 272-280 ◽  
Author(s):  
Luz E. Vera-Avila ◽  
Erika García-Salgado ◽  
Martha P. García de Llasera ◽  
Araceli Peña-Alvarez
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Interaction ◽  
Bovine Serum ◽  
Sol Gel ◽  
Binding Characteristics ◽  
Interaction Studies ◽  
Gel Glasses

Molecular Interaction of Hemorrheologic Agent, Pentoxifylline with Bovine Serum Albumin: An Approach to Investigate the Drug Protein Interaction Using multispectroscopic, Voltammetry and Molecular Modelling Techniques

2019 ◽  
Vol 233 (7) ◽  
pp. 973-994
Author(s):  
Mahanthappa Mallappa ◽  
Mohammed Azharuddin Savanur ◽  
Babu Giriya Gowda ◽  
R.S. Vishwanth ◽  
Bijesh Puthusseri
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Changes ◽  
Protein Interaction ◽  
Molecular Modelling ◽  
Bovine Serum ◽  
Cd Spectroscopy ◽  
Fluorescence Studies ◽  
Modelling Techniques ◽  
Uv Visible

Abstract The interaction between pentoxifylline (PTX) and bovine serum albumin (BSA) was studied under physiological condition by spectroscopic, voltammetry and molecular modelling techniques. The results of fluorescence studies revealed that the quenching mechanism of BSA by PTX was a static procedure. Binding constant of PTX-BSA was calculated and its value found to be 8.895 × 104 M−1, which is in close agreement with the results obtained from UV-Visible and voltammetry approach. The negative values of thermodynamic parameters (ΔG, ΔH and ΔS) indicated that van der Waals force and hydrogen bonding play major roles in the interaction of PTX with BSA. Based on Forster’s theory of non-radiation energy transfer, the binding distance (r) between the donor (BSA) and acceptor (PTX) was found to be 5.38 nm (298 K). The results of UV-Visible and circular dichroism (CD) spectroscopy showed that PTX interacts with BSA and induces conformational changes by reducing the α-helix content. The results of the UV-visible and voltammetry studies were further verified by the molecular docking method. Molecular modelling studies revealed possible residues involved in the drug-protein interaction and indicated that PTX binds to Site IIA of BSA.

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