Cationic double chained metallosurfactants: synthesis, aggregation, cytotoxicity, antimicrobial activity and their impact on the structure of bovine serum albumin. Issue 25 (15th June 2018)

• Record Type: Journal Article
• Authors: Kaur, Gurpreet; Garg, Preeti; Kaur, Baljinder; Chaudhary, Ganga Ram; Kumar, Sandeep; Dilbaghi, Neeraj; Hassan, P. A.; Gawali, Santosh L.
• Is Part Of: Soft matter. Volume 14:Issue 25(2018)
• Page Start: 5306
• Page End: 5318
• Publication Date: 2018-06-15
• Subjects: Soft condensed matter -- Periodicals; 530.413
• DOI: 10.1039/c8sm00535d
• Languages: English
• ISSNs: 1744-683X

Abstract

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