Use of zwitterionic detergents for the separation of closely related peptides by capillary electrophoresis.
Capillary electrophoresis incorporating hydrophobic selectivity is shown to be a powerful technique for separating closely related peptide species. In this work, hydrophobic interaction was induced through the addition of suitable amounts of a zwitterionic detergent (N-dodecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate) and further modified with organic solvents. A neutral, hydrophilic-coated capillary was used to minimize electroosmotic flow. Two test solutes, Met15- and Leu15-gastrin, were employed to probe hydrophobic selectivity with various electrophoretic 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 highest hydrophobic selectivity among the conditions studied. The zwitterionic detergent approach was also briefly compared to the use of non-ionic detergents for hydrophobic selectivity.
Barnett Institute, Northeastern University, Boston, MA 02115.
K F
KF
Greve
W
W
Nashabeh
B L
BL
Karger
D000595:Amino Acid Sequence; D000818:Animals; D003902:Detergents; D004586:Electrophoresis / Q000379:methods*; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000302:isolation & purification*; D000644:Quaternary Ammonium Compounds; D013552:Swine
D003902:Detergents; D010455:Peptides; D000644:Quaternary Ammonium Compounds; C034730:zwittergent 3-12