Influence of BSA on micelle formation of SDBS and CPC: An experimental–theoretical approach of its binding properties

Vivek Sharma, Plinio Cantero-López, Osvaldo Yañez-Osses, Cecilia Rojas-fuentes, Ashish Kumar

Resultado de la investigación: Article

1 Cita (Scopus)

Resumen

Serum albumins play important roles in many physiological functions and serve as transporters in the transportation and distribution of endogenous and exogenous substances. Ligand-protein interaction experiments and computational approach have great significance in gaining fundamental binding characteristic of the complex. This work reports the interactions of Bovine serum albumin (BSA) with Sodium dodecyl benzene sulfonate (SDBS) and Cetyl pyridinium chloride (CPC), that have been measured by electrical conductivity, spectrophotometric and computational studies. Micellization of ionic surfactants is delayed by concentration of BSA and the temperature also restricted the same. Binding efficiency of BSA to that of ionic surfactants has been determined by absorbance spectroscopy. Computational studies confirmed the presence of 8 binding sites of BSA for SDBS and CPC. It was found that the low energy binding sites of BSA were more preferred by ionic surfactants.

Idioma originalEnglish
Páginas (desde-hasta)443-451
Número de páginas9
PublicaciónJournal of Molecular Liquids
Volumen271
DOI
EstadoPublished - 1 dic 2018

Huella dactilar

Micelles
Bovine Serum Albumin
sulfonates
albumins
serums
Chlorides
Benzene
micelles
Surface active agents
chlorides
benzene
Sodium
sodium
Binding sites
Surface-Active Agents
Micellization
surfactants
Binding Sites
Ligands
Spectroscopy

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Atomic and Molecular Physics, and Optics
  • Condensed Matter Physics
  • Spectroscopy
  • Physical and Theoretical Chemistry
  • Materials Chemistry

Citar esto

Sharma, Vivek ; Cantero-López, Plinio ; Yañez-Osses, Osvaldo ; Rojas-fuentes, Cecilia ; Kumar, Ashish. / Influence of BSA on micelle formation of SDBS and CPC : An experimental–theoretical approach of its binding properties. En: Journal of Molecular Liquids. 2018 ; Vol. 271. pp. 443-451.
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Influence of BSA on micelle formation of SDBS and CPC : An experimental–theoretical approach of its binding properties. / Sharma, Vivek; Cantero-López, Plinio; Yañez-Osses, Osvaldo; Rojas-fuentes, Cecilia; Kumar, Ashish.

En: Journal of Molecular Liquids, Vol. 271, 01.12.2018, p. 443-451.

Resultado de la investigación: Article

TY - JOUR

T1 - Influence of BSA on micelle formation of SDBS and CPC

T2 - An experimental–theoretical approach of its binding properties

AU - Sharma, Vivek

AU - Cantero-López, Plinio

AU - Yañez-Osses, Osvaldo

AU - Rojas-fuentes, Cecilia

AU - Kumar, Ashish

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AB - Serum albumins play important roles in many physiological functions and serve as transporters in the transportation and distribution of endogenous and exogenous substances. Ligand-protein interaction experiments and computational approach have great significance in gaining fundamental binding characteristic of the complex. This work reports the interactions of Bovine serum albumin (BSA) with Sodium dodecyl benzene sulfonate (SDBS) and Cetyl pyridinium chloride (CPC), that have been measured by electrical conductivity, spectrophotometric and computational studies. Micellization of ionic surfactants is delayed by concentration of BSA and the temperature also restricted the same. Binding efficiency of BSA to that of ionic surfactants has been determined by absorbance spectroscopy. Computational studies confirmed the presence of 8 binding sites of BSA for SDBS and CPC. It was found that the low energy binding sites of BSA were more preferred by ionic surfactants.

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KW - Binding efficiency

KW - Ionic surfactants

KW - Ligand-protein interactions

KW - Micellization

KW - Molecular docking

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