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Molecular interaction of cationic gemini surfactant with bovine serum albumin: A spectroscopic and molecular docking study

Paper ID Volume ID Publish Year Pages File Format Full-Text
34708 45040 2014 8 PDF Available
Title
Molecular interaction of cationic gemini surfactant with bovine serum albumin: A spectroscopic and molecular docking study
Abstract

•DBG quenches the fluorescence intensity of BSA and changes its conformation.•Quenching follows the static mechanism.•DBG binds to the Arg-194, Arg-198 and Arg-217 residues of BSA.

Herein, we report the effect of N,N′-bis(dodecyloxycarbonylmethyl)-N,N,N′,N′-tetramethyl-1,2-ethanediammonium dibromide (dodecyl betainate gemini or DBG) on the structure and function of bovine serum albumin (BSA) by using fluorescence, time resolved fluorescence, circular dichroism and dynamic light scattering techniques. The Stern–Volmer quenching constants KSV and the corresponding thermodynamic parameters viz ΔH, ΔG and ΔS have been estimated by the fluorescence quenching method. The results indicated that DBG binds spontaneously with BSA through hydrophobic interaction. Time resolved fluorescence data show that the quenching follows the static mechanism pathway. It can be seen from far-UV CD spectra that the α-helical network of BSA is disrupted and its content increases from 71% to 79% at lower concentrations which again decreases to 38% at higher concentration. DLS measurements suggested that hydrodynamic radius (Rh) decreases in the presence of 30 and 40 μM of DBG while it increases when the concentration of DBG was 70 and 100 μM. The molecular docking study indicated that DBG is embedded into subdomain IIA of BSA and binds with the R-914, R-195 and R-217 residues by hydrogen bonding and by hydrophobic interaction.

Keywords
Bovine serum albumin; Gemini surfactant; Quenching; Fluorescence; Interaction; Modelling
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Molecular interaction of cationic gemini surfactant with bovine serum albumin: A spectroscopic and molecular docking study
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 49, Issue 4, April 2014, Pages 623–630
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
Online Support
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