Molecular features of nonionic detergents involved in the binding kinetics and solubilization efficiency, as studied in model (Langmuir films) and biological (Erythrocytes) membranes

[Display omitted] •Brij detergents are stronger (erythrocyte) membrane solubilizers than Triton X-100.•Brij shows low effective detergent/lipid molar ratios for hemolysis (Re  Brij 98 > TX-100. The effect of the nonionic detergents Brij-98 and Brij-58 over human erythrocytes was studied through q...

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Bibliographic Details
Published in:Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2018-06, Vol.166, p.152-160
Main Authors: Casadei, Bruna Renata, Domingues, Cleyton Crepaldi, Clop, Eduardo M., Couto, Verônica Muniz, Perillo, Maria Angelica, de Paula, Eneida
Format: Article
Language:English
Subjects:
Brij
Erythrocyte membranes
Monolayers
Nonionic detergents
Solubilization
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Summary:[Display omitted] •Brij detergents are stronger (erythrocyte) membrane solubilizers than Triton X-100.•Brij shows low effective detergent/lipid molar ratios for hemolysis (Re  Brij 98 > TX-100. The effect of the nonionic detergents Brij-98 and Brij-58 over human erythrocytes was studied through quantitative hemolysis and in Langmuir films. Hemolytic tests revealed that Brijs are stronger membrane solubilizers than Triton X-100 (TX-100), with effective detergent/lipid ratios of 0.18 and 0.37 for Brij-98 and Brij-58, respectively. Experiments with Langmuir films provided significant information on the kinetics and thermodynamics of detergent-membrane interaction. The adsorption (ka) and desorption (kd) rate constants of Brijs were lower than those of TX-100. In the case of ka, that is probably due to their larger hydrophilic head (with twice (20) the oxyethylene units of TX-100). As for the thermodynamic binding constant, the linear and longer hydrophobic acyl chains of Brijs favor their stabilization in-between the lipids, through London van der Waals forces. Consequently, Kb,m values of Brij-98 (12,500 M−1) and Brij-58 (19,300 M−1) resulted higher than TX-100 (7500 M−1), in agreement with results from the hemolytic tests. Furthermore, Brij-58 binds with higher affinity than Brij-98 to bilayers and monolayers, despite its shorter (palmitic) hydrocarbon chain, showing that unsaturation restrains the detergent insertion into these environments. Our results provide significant information about the mechanism of interaction between Brijs and membranes, supporting their distinct solubilization effect.
ISSN:0927-7765
1873-4367
DOI:10.1016/j.colsurfb.2018.03.012