title: Towards determination of the structure of the Saccharomyces cerevisiae a-factor: an acylated pentadecapeptide blocks a-factor activity.
abstract: Putative a-factor peptides YIIKGVFWADP, YIIKGVFWANP, YIIKGLFWADP, YIIKGLFWANP, YIIKGVFWDPA, and YIIKGVFWDPACVIA and several peptide derivatives were synthesized and were found to be inactive in growth arrest assays, yet they blocked the activity of biological a-factor. Antagonism was greatest with YIIKGVFWDPAC(palmitoyl)VIA. Thus, the structure of a-factor may be a lipopeptide resembling this palmitoylated pentadecapeptide.
authors.affiliation: Department of Microbiology, University of Tennessee, Knoxville 37996.
authors.forename: J M
authors.initials: JM
authors.lastname: Becker
authors.forename: S
authors.initials: S
authors.lastname: Marcus
authors.forename: B
authors.initials: B
authors.lastname: Kundu
authors.forename: P
authors.initials: P
authors.lastname: Shenbagamurthi
authors.forename: F
authors.initials: F
authors.lastname: Naider
mesh_terms: D000215:Acylation; D000595:Amino Acid Sequence; D000072235:Mating Factor; D009842:Oligopeptides / Q000494:pharmacology; D010455:Peptides / Q000037:antagonists & inhibitors / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000502:physiology*; D013329:Structure-Activity Relationship
chemical_list: D009842:Oligopeptides; D010455:Peptides; D000072235:Mating Factor