Title: | Lipid-mediated a-factor interactions with artificial membranes |
Author(s): | Epand RM; Naider F; Becker JM; |
Address: | "Department of Biochemistry, McMaster University Health Sciences Center, Hamilton, Ontario, Canada" |
DOI: | 10.1016/0076-6879(95)50071-5 |
ISSN/ISBN: | 0076-6879 (Print) 0076-6879 (Linking) |
Abstract: | Our understanding of the cellular export of a-factor and its interaction with the receptor do not yet allow for a description of the phenomena on a molecular level. Synthesis of a-factor analogs and biophysical studies of the lipopeptides in the presence of artificial membranes provide insights which can be analyzed with respect to the biological potency of the molecules. It is through the study of the interaction of the lipopeptides with membranes at varying levels of complexity that we will be able to develop a molecular description of the biological processes |
Keywords: | *Alkyl and Aryl Transferases Amino Acid Sequence Farnesol Farnesyltranstransferase Indicators and Reagents *Lipid Bilayers Mating Factor Molecular Sequence Data Peptides/chemical synthesis/*chemistry/metabolism Pheromones/chemistry Polyisoprenyl Phosphate; |
Notes: | "MedlineEpand, R M Naider, F Becker, J M eng GM46520/GM/NIGMS NIH HHS/ Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1995/01/01 Methods Enzymol. 1995; 250:169-86. doi: 10.1016/0076-6879(95)50071-5" |