Cationic double chained metallosurfactants: Synthesis, aggregation, cytotoxicity, antimicrobial activity and their impact on structure of Bovine serum albumin

August 13, 2018

Title

Cationic double chained metallosurfactants: Synthesis, aggregation, cytotoxicity, antimicrobial activity and their impact on structure of Bovine serum albumin

Author

Gurpreet Kaur, Preeti Garg, Baljinder Kaur, Ganga Ram Chaudhary, Sandeep Kumar, N Dilbaghi, Puthusserickal Hassan, Santosh L Gawali

Year

2018

Journal

Soft Matter

Abstract

Bovine Serum Albumin (BSA) is one of the most copious and significant blood proteins with dynamic structure. The understanding of the structural functionality of BSA and interaction with metal ions is desired for various biological functions. Herein, we three different metallosurfactants containing transition metals and same hydrophobic tail were engaged to investigate the structural transition of BSA. The metallosurfactants have been prepared by combination of metal ions (M= Fe, Co and Ni) with cetylpyridinium chloride surfactant via ligand insertion method and were characterized by elemental, FTIR, 1H-NMR, and thermogravimetric analysis (TGA). The obtained results reveal that insertion of metal ion perturbs the aggregation behavior of surfactant. Incorporation of metal-ion have been found to decrease the CMC value of surfactant that has been supported by conductivity surface tension and small angle Xray Scattreing (SAXS). These metallosurfactants were employed to study the interaction and binding mechanism of BSA under physiological conditions. The SDS-PAGE analysis points out a weak effect of metallosurfactant on the primary structure of BSA, whereas CD spectra implied the significant change in secondary structure with the decreased α-helical content of BSA. Fluorescence spectroscopy alludes the effect of metallosurfactants on tertiary structure of BSA whereas absorption spectra demonstrated static quenching with a blue shift in presence of metallosurfactants. Moreover, unfolding of BSA in presence of metallosurfactants has also been confirmed by SAXS studies. The overall results indicate that insertion of the metal ion in framework of surfactant structure enhances its protein binding/folding/unfolding abilities that would be helpful in clinical as well as in life sciences. Keywords: metallosurfactants; BSA; protein binding; antimicrobial studies; haemolysis

Instrument

J-815

Keywords

Circular dichroism, Secondary structure, Chemical stability, Biochemistry