| Title: | Structure-activity relationships in the dodecapeptide alpha factor of Saccharomyces cerevisiae |
| Author(s): | Shenbagamurthi P; Baffi R; Khan SA; Lipke P; Pousman C; Becker JM; Naider F; |
| ISSN/ISBN: | 0006-2960 (Print) 0006-2960 (Linking) |
| Abstract: | "Ten analogues of His-Trp-Leu-Gln-Leu-Lys-Pro-Gly-Gln-Pro-Met-Tyr, the dodecapeptide alpha factor of Saccharomyces cerevisiae, were synthesized by conventional solution phase techniques and purified by using high-performance liquid chromatography. The dodecapeptide was also synthesized attached at its carboxyl terminus to poly(ethylene oxide), a macromolecular protecting group. Analogues in which Lys6 or His1 was modified exhibited high biological activity as evidenced by their ability to elicit aberrant morphologies in a cells of S. cerevisiae. These results suggest that neither a free alpha-amine nor a protonatable side chain at position 6 is necessary for biological activity of the dodecapeptide alpha factor. Although Ala2- and Phe2-dodecapeptides were not biologically active, they competed with the natural alpha factor and several active analogues. Thus binding of the alpha factor is not sufficient to elicit a biological response; it appears that the side chain in position 2 is critical for triggering morphological alterations in a cells" |
| Keywords: | "Chromatography, High Pressure Liquid Mating Factor *Peptides/pharmacology Saccharomyces cerevisiae/*drug effects Structure-Activity Relationship;" |
| Notes: | "MedlineShenbagamurthi, P Baffi, R Khan, S A Lipke, P Pousman, C Becker, J M Naider, F eng GM-22086/GM/NIGMS NIH HHS/ GM-22087/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1983/03/01 Biochemistry. 1983 Mar 1; 22(5):1298-304. doi: 10.1021/bi00274a047" |
