Electrophoretic behavior of L- and D-alanine-scanning analogs of a yeast tridecapeptide pheromone in a fused-silica capillary.
Electrophoretic behavior of synthetic tridecapeptide diastereomers has been systematically investigated using a series of L-Ala- and D-Ala-scanning analogs of [Nle12] alpha-factor [WHWLQLKPGQP(Nle)Y], a tridecapeptide mating pheromone of Saccharomyces cerevisiae. The effects of buffer pH, buffer concentration, voltage, and temperature on diastereomer separation were tested. Among 13 pairs of diastereomers, those with L-Ala/D-Ala replacement in the middle of the peptide chain exhibited much higher diastereomeric resolution than those with identical replacement near the peptide termini. The fact that D-Ala9 and D-Ala12 homologs exhibited abnormal mobility differences compared to their L-diastereomers is probably related to the conformational restriction imposed by a Pro-D-Ala sequence. The results on the alpha-factor analogs represent the first observations of the influence of peptide secondary structure on mobility during capillary electrophoresis.
Zhang
Y L
YL
Department of Chemistry, College of Staten Island of the City University of New York 10314, USA.
Becker
J M
JM
Naider
F R
FR
D000595:Amino Acid Sequence; D002021:Buffers; D019075:Electrophoresis, Capillary / Q000379:methods*; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D010675:Pheromones / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000737:chemistry*; D013237:Stereoisomerism; D013696:Temperature
D002021:Buffers; D010455:Peptides; D010675:Pheromones