| Title: | Electrophoretic behavior of L- and D-alanine-scanning analogs of a yeast tridecapeptide pheromone in a fused-silica capillary |
| Author(s): | Zhang YL; Becker JM; Naider FR; |
| Address: | "Department of Chemistry, College of Staten Island of the City University of New York 10314, USA" |
| ISSN/ISBN: | 0003-2697 (Print) 0003-2697 (Linking) |
| Abstract: | "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" |
| Keywords: | "Amino Acid Sequence Buffers Electrophoresis, Capillary/*methods Hydrogen-Ion Concentration Molecular Sequence Data Peptides/*chemistry Pheromones/*chemistry Saccharomyces cerevisiae/*chemistry Stereoisomerism Temperature;" |
| Notes: | "MedlineZhang, Y L Becker, J M Naider, F R eng GM-22086/GM/NIGMS NIH HHS/ GM-22087/GM/NIGMS NIH HHS/ Research Support, U.S. Gov't, P.H.S. 1996/10/15 Anal Biochem. 1996 Oct 15; 241(2):220-7. doi: 10.1006/abio.1996.0403" |
