| Title: | Conformational analysis of [D-Ala9]alpha-factor and [L-Ala9]alpha-factor in solution and in the presence of lipid |
| Author(s): | Gounarides JS; Broido MS; Becker JM; Naider FR; |
| Address: | "Department of Chemistry, Hunter College, City University of New York, New York 10021" |
| ISSN/ISBN: | 0006-2960 (Print) 0006-2960 (Linking) |
| Abstract: | "The conformations in solution and in the presence of lipid vesicles of [D-Ala9] and [L-Ala9] analogues of the alpha-factor (WHWLQLKPGQPMY) from the yeast Saccharomyces cerevisiae were examined by NMR spectroscopy. Although both peptides are flexible molecules, NOE and NH d delta/dT data indicate that the [D-Ala9]alpha-factor analogue in DMSO and aqueous solution adopts a type II beta-turn about residues 8 and 9. In contrast, various NMR parameters for the less active [L-Ala9] analogue do not provide evidence for a regular secondary structure in solution. Transfer NOE data indicate that for both peptides binding to the lipid is strongest for the N-terminal residues. The C-terminus of the [D-Ala9] analogue appears to be more constrained in the bound state than the C-terminus of the [L-Ala9] analogue. This result is consistent with transfer NOE evidence that the type II beta-turn conformation of the [D-Ala9]alpha-factor is maintained in the lipid bound state" |
| Keywords: | Amino Acid Sequence Lipids/*pharmacology Liposomes/pharmacology Magnetic Resonance Spectroscopy Mating Factor Molecular Conformation Molecular Sequence Data Peptides/*chemistry/drug effects Pheromones/*chemistry Phosphatidylcholines/pharmacology Saccharom; |
| Notes: | "MedlineGounarides, J S Broido, M S Becker, J M Naider, F R eng GM22086/GM/NIGMS NIH HHS/ GM22087/GM/NIGMS NIH HHS/ Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1993/01/26 Biochemistry. 1993 Jan 26; 32(3):908-17. doi: 10.1021/bi00054a023" |
