Open-tubular electrochromatographic characterization of synthetic peptides.
The open-tubular electrochromatographic (OT-CEC) migration behavior of a series of peptides, based on a common structural feature, has been characterized using two different types of chemically modified etched capillaries. The organic moieties immobilized onto the capillary inner surface were n-butylphenyl and cholesterol-10-undecenaoate, respectively. The structure-migration behavior of this set of peptides has been studied at several pH values and with methanol at different concentrations as an organic solvent modifier of the buffer electrolyte composition. By comparing the structural properties of the peptides, such as their amino acid sequences, charge-to-mass ratios and intrinsic hydrophobicities to their migrational behavior, the relative contribution of electrophoretic and chromatographic mobility to the overall migration times, elution order, and selectivity has been determined. Moreover, the experimental data provide important insight into procedures that can be used to modulate the separation of peptides in OT-CEC through variation of the composition of the electrolyte buffer as well as via the properties of the bonded organic moiety.
Pesek
Joseph J
JJ
Department of Chemistry, San Jose State University, San Jose, CA, USA.
Matyska
Maria T
MT
Dawson
G Brent
GB
Chen
Jenny I-Chen
JI
Boysen
Reinhard I
RI
Hearn
Milton T W
MT
D000595:Amino Acid Sequence; D002784:Cholesterol / Q000737:chemistry*; D020374:Chromatography, Micellar Electrokinetic Capillary; D004573:Electrolytes / Q000737:chemistry*; D019075:Electrophoresis, Capillary; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*
D004573:Electrolytes; D010455:Peptides; D002784:Cholesterol