Interaction of Myoglobin with Cationic and Nonionic Surfactant in Phosphate Buffer Media

By Satyajit Mondal, Maria Luz Raposo, Gerardo Prieto, Soumen Ghosh

July 28, 2017

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Title

Interaction of Myoglobin with Cationic and Nonionic Surfactant in Phosphate Buffer Media

Author

Satyajit Mondal, Maria Luz Raposo, Gerardo Prieto, Soumen Ghosh

Year

2016

Journal

Journal of Chemical and Engineering Data

Abstract

Interaction of myoglobin with cationic surfactants hexadecyltrimethylammonium bromide (HTAB), gemini surfactant 16-2-16 (dimethylene-1,2-bis(hexadecyldimethylammonium bromide)) and nonionic surfactant Mega 10 (N-decanoyl-N-methylglucamine) have been studied in phosphate buffer at pH 7.4 using surface tension, UV–visible, fluorescence, and circular dichroism spectroscopies and differential scanning calorimetry. With increasing concentration of HTAB, metal ion of the heme group changes its spin states; but in case of 16-2-16 and Mega 10, spin change does not occur. Fluorescence spectra clearly denote the unfolding process in HTAB media. With increasing HTAB concentration, α-helicity of myoglobin decreases with the appearance of β-sheet and random coil more rapidly than other two surfactants. Melting temperature of myoglobin is reduced drastically upon interaction with HTAB than their corresponding gemini and nonionic surfactants.

Full Article

http://pubs.acs.org/doi/abs/10.1021/acs.jced.5b00858

Instrument

J-815

Keywords

Circular dichroism, Protein folding, Secondary structure, Thermodynamics, Biochemistry