TRIS-STABILIZED PROTEIN AND CATIONIC SURFACTANT: SOFT MODIFICATION OF SIZE AND ELECTROKINETIC POTENTIAL OF BSA GLOBULES USING CYCLODEXTRIN
Rubrics: 1. CHEMISTRY
Authors:
1.
Kazan National Research Technological University
2.
KNITU
Type:
Article
Pages:
from 11
to 18
Status:
Published
Received:
31.01.2026
Accepted:
05.02.2026
Published:
26.02.2026
Language:
Russian
Keywords:
PROTEIN-SURFACTANT INTERACTIONS, CYCLODEXTRIN-SURFACTANT INCLUSION COMPLEX, BOVINE SERUM ALBUMIN, DODECYLTRIMETHYLAMMONIUM BROMIDE, (2-HYDROXYPROPYL)-β-CYCLODEXTRIN, TRIS-STABILIZED PROTEIN, CONFORMATION, X-POTENTIAL, TRYPTOPHAN DEHYDROPHOBIZATION
Abstract:
Protein conformation can be controlled using surfactants. Cyclodextrins form inclusion complexes with surfactants, whose behavior differs from that of conventional surfactants in water. To elucidate the role of different types of interactions in the surfactant-protein-cyclodextrin system, changes in size, x-potential, and tryptophan fluorescence of associates of the cationic surfactant dodecyltrimethylammonium bromide (DTAB) with bovine serum albumin (BSA) in the presence of (2-hydroxypropyl)-b-cyclodextrin (2HPβCD) in Tris-buffered aqueous solutions (pH=7.3) have been studied using dynamic light scattering, electrophoresis, and fluorescence spectrometry. 2HPβCD forms a stable stoichiometric complex with DTAB, and in the presence of 2HPβCD, the conformation of the protein in the system is controlled by the 2HPβCD:DTAB ratio. If there are no surfactant micelles in the system, the addition of 2HPβCD causes the protein to decompactify, and at 2HPβCD: DTAB<1, a bimodal distribution of particle sizes is observed, which transitions to a unimodal distribution strictly at a ratio of 2HPβCD:DTAB=1, when only particles larger than in the absence of 2HPβCD remain. Conversely, if there are surfactant micelles in the system, the addition of 2HPβCD leads to compression of the protein-surfactant associates. Fluorescence spectroscopy data showed that conformational changes upon the addition of 2HPβCD are accompanied by dehydrophobization of the tryptophan environment within the BSA macromolecule. The dependence of the electrokinetic potential of protein-surfactant associates on the 2HPβCD:DTAB ratio is determined by the DTAB:BSA ratio. In this article, we aim to link the observed behavior with intermolecular interactions in the system.
Protein conformation can be controlled using surfactants. Cyclodextrins form inclusion complexes with surfactants, whose behavior differs from that of conventional surfactants in water. To elucidate the role of different types of interactions in the surfactant-protein-cyclodextrin system, changes in size, x-potential, and tryptophan fluorescence of associates of the cationic surfactant dodecyltrimethylammonium bromide (DTAB) with bovine serum albumin (BSA) in the presence of (2-hydroxypropyl)-b-cyclodextrin (2HPβCD) in Tris-buffered aqueous solutions (pH=7.3) have been studied using dynamic light scattering, electrophoresis, and fluorescence spectrometry. 2HPβCD forms a stable stoichiometric complex with DTAB, and in the presence of 2HPβCD, the conformation of the protein in the system is controlled by the 2HPβCD:DTAB ratio. If there are no surfactant micelles in the system, the addition of 2HPβCD causes the protein to decompactify, and at 2HPβCD: DTAB<1, a bimodal distribution of particle sizes is observed, which transitions to a unimodal distribution strictly at a ratio of 2HPβCD:DTAB=1, when only particles larger than in the absence of 2HPβCD remain. Conversely, if there are surfactant micelles in the system, the addition of 2HPβCD leads to compression of the protein-surfactant associates. Fluorescence spectroscopy data showed that conformational changes upon the addition of 2HPβCD are accompanied by dehydrophobization of the tryptophan environment within the BSA macromolecule. The dependence of the electrokinetic potential of protein-surfactant associates on the 2HPβCD:DTAB ratio is determined by the DTAB:BSA ratio. In this article, we aim to link the observed behavior with intermolecular interactions in the system.
Keywords:
PROTEIN-SURFACTANT INTERACTIONS, CYCLODEXTRIN-SURFACTANT INCLUSION COMPLEX, BOVINE SERUM ALBUMIN, DODECYLTRIMETHYLAMMONIUM BROMIDE, (2-HYDROXYPROPYL)-β-CYCLODEXTRIN, TRIS-STABILIZED PROTEIN, CONFORMATION, X-POTENTIAL, TRYPTOPHAN DEHYDROPHOBIZATION
PROTEIN-SURFACTANT INTERACTIONS, CYCLODEXTRIN-SURFACTANT INCLUSION COMPLEX, BOVINE SERUM ALBUMIN, DODECYLTRIMETHYLAMMONIUM BROMIDE, (2-HYDROXYPROPYL)-β-CYCLODEXTRIN, TRIS-STABILIZED PROTEIN, CONFORMATION, X-POTENTIAL, TRYPTOPHAN DEHYDROPHOBIZATION
