Effect of pH and surfactant on the protein: A perspective from theory and experiments

•BSA shows turbidity at below CMC of SDS at pH 4.0 but turbidity over after CMC.•Various analyses bring out the interesting information at pHs 4.0, 4.7 & 7.0.•BSA starts to unfold by addition of SDS till CMC after CMC again folding occurs.•AFM imaging shows the structural change in the process o...

Full description

Saved in:
Bibliographic Details
Published in:International journal of biological macromolecules 2018-02, Vol.107 (Pt B), p.1519-1527
Main Authors: Srivastava, Rachana, Alam, Md. Sayem
Format: Article
Language:English
Subjects:
Animals
Bovine serum albumin
Cattle
Circular Dichroism
Electric Conductivity
Hydrogen-Ion Concentration
Hydrophobic interaction and electrostatic interaction
Micelles
Microscopy, Atomic Force
Molecular Docking Simulation
Protein denaturation
Protein Folding
Protein Structure, Secondary
Serum Albumin, Bovine - chemistry
Sodium dodecyl sulfate
Spectrometry, Fluorescence
Spectrophotometry, Ultraviolet
Surface-Active Agents - pharmacology
Time Factors
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:•BSA shows turbidity at below CMC of SDS at pH 4.0 but turbidity over after CMC.•Various analyses bring out the interesting information at pHs 4.0, 4.7 & 7.0.•BSA starts to unfold by addition of SDS till CMC after CMC again folding occurs.•AFM imaging shows the structural change in the process of denaturation at pH 4.0.•Denaturation of BSA can partially control by the higher concentration of SDS. In the present study, we are aimed to explore the bovine serum albumin (BSA) and sodium dodecyl sulfate (SDS) the interaction that can readily show the consequence of the change in concentration of protein with surfactants’ various concentration and the different pH’s, 4.0, 4.7, 7.0 of the medium through the many spectroscopic techniques. The BSA and SDS denaturation fully influenced by the pH. The results interpreted in terms of electrostatic and hydrophobic contributions to the stability of different phases formed in the system. Critical Micelle Concentration (CMC) of surfactant is influenced the protein folding and unfolding. The molecular docking supports the experiment data. This study demonstrates that the above and below the CMC of surfactant can significantly alter the binding interaction with the protein.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2017.10.019