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 original | English |
|---|---|
| Páginas (desde-hasta) | 443-451 |
| Número de páginas | 9 |
| Publicación | Journal of Molecular Liquids |
| Volumen | 271 |
| DOI | |
| Estado | Published - 1 dic 2018 |
Huella dactilar
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
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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
PY - 2018/12/1
Y1 - 2018/12/1
N2 - 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.
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.
KW - Albumin
KW - Binding efficiency
KW - Ionic surfactants
KW - Ligand-protein interactions
KW - Micellization
KW - Molecular docking
UR - http://www.scopus.com/inward/record.url?scp=85052920413&partnerID=8YFLogxK
U2 - 10.1016/j.molliq.2018.09.003
DO - 10.1016/j.molliq.2018.09.003
M3 - Article
AN - SCOPUS:85052920413
VL - 271
SP - 443
EP - 451
JO - Journal of Molecular Liquids
JF - Journal of Molecular Liquids
SN - 0167-7322
ER -