Kf. Greve et al., USE OF ZWITTERIONIC DETERGENTS FOR THE SEPARATION OF CLOSELY-RELATED PEPTIDES BY CAPILLARY ELECTROPHORESIS, Journal of chromatography, 680(1), 1994, pp. 15-24
Capillary electrophoresis incorporating hydrophobic selectivity is sho
wn to be a powerful technique for separating closely related peptide s
pecies. In this work, hydrophobic interaction was induced through the
addition of suitable amounts of a zwitterionic detergent dodecyl-N,N-d
imethyl-3-ammonio-1-propanesulfonate) and further modified with organi
c solvents. A neutral, hydrophilic-coated capillary was used to minimi
ze electroosmotic flow. Two test solutes, Met(15)- and Leu(15)-gastrin
, were employed to probe hydrophobic selectivity with various electrop
horetic conditions. The nature and concentration of the detergent and
the organic modifier were varied to adjust the selectivity. Operation
near the critical micelle concentration of the zwitterionic detergent
in the presence of acetonitrile or various alcohols produced the highe
st hydrophobic selectivity among the conditions studied. The zwitterio
nic detergent approach was also briefly compared to the use of non-ion
ic detergents for hydrophobic selectivity.