Our group has been active in developing techniques for the efficient synthesis of farnesylated peptides which are then subjected to biophysical and biochemical investigation. The biological activity of peptide hormones implies that these molecules assume a specific conformation when they bind to their target receptor. We have actively pursued the biologically active conformation of the a -factor using circular dichroism, nuclear magnetic resonance and vibrational circular dichroism studies. Both linear analogs of the pheromone and analogs with covalent constraints have been prepared and studied. Toward this end we have participated in purifying this receptor to homogeneity and have been synthesizing fragments of the receptor for biophysical analysis using circular dichroism and nuclear magnetic resonance spectroscopy in solution and the solid state.
Peptides are sources of amino acids and nitrogen for cells.
We are studying the uptake of peptide by single cell eukaryotes such as the yeast Saccharomyces cerevisiae and the pathogenic fungus Candida albicans . These studies resulted in the discovery of the PTR family of peptide transporters which are now known to exist in human intestine and human kidney. These studies provide fundamental information on molecular transport phenomena and may be useful in the design of antifungal drugs. References B. Arshava, M. Breslav, O. Antohi, R. E. Stark, J. R. Garbow, J.M. Becker and F. Naider. H. Xie, J. M. Becker, R. A. Gibbs, and F. Naider.