Quantitative studies on the adsorption of proteins to the bare silica wallin capillary electrophoresis III: Effects of adsorbed surfactants on quenching the interaction
L. Castelletti et al., Quantitative studies on the adsorption of proteins to the bare silica wallin capillary electrophoresis III: Effects of adsorbed surfactants on quenching the interaction, J CHROMAT A, 894(1-2), 2000, pp. 281-289
The efficacy of two classes of surfactants, non-ionic and zwitterionic, in
quenching the interaction of proteins with the naked silica wall in capilla
ry electrophoresis, is evaluated. The class of non-ionic detergents is foun
d to be rather inefficient in preventing protein binding to the fused-silic
a surface, since large amounts (up to 10%) are required for reducing such i
nteractions by 90%. Conversely, zwittergents appear to be much more efficie
nt, since, in the case of sulphobetain SB-16, 90% binding inhibition is ach
ieved at a concentration of surfactant of only 0.3%. In this last case, it
is found that the binding inhibition closely follows the values of critical
micellar concentrations (CMCs) of the various surfactants, those having th
e lowest CMC value exhibiting the highest inhibition power. The CMC values
also follow a hydrophobicity scale, suggesting that the most hydrophobic zw
ittergents are the ones that shield more efficiently the silica surface. (C
) 2000 Elsevier Science BN. All rights reserved.