Synthesis of Fmoc-protected dicarboxyglutamic acid and its use in solid phase peptide synthesis

CHED 234

James W. Nelson, jnelson@udel.edu, Lisa A Capriotti, lcap@udel.edu, and Joel P. Schneider, schneijp@udel.edu. Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716-2522
Osteocalcin, a protein component of bone, is believed to bind tightly to the surface of hydroxyapatite due to the presence of three dicarboxylated glutamic acid residues in its amine terminal α-helix. Despite its hypothesized affinity for hydroxyapatite, dicarboxyglutamic acid has not been widely used in de novo peptide design. In order to create an α-helical peptide which binds to bone, we designed a short peptide containing five dicarboxyglutamic acid residues. The behavior and characteristics of this peptide as determined through circular dichroism spectroscopy will be discussed. To this end, it will be necessary to describe the synthesis of the dicarboxylated glutamic acid residue for the Fmoc-based synthesis of the peptide. This synthesis was undertaken by using L-serine as a starting material.
 

Undergraduate Research Poster Session: Organic Chemistry
2:00 PM-4:00 PM, Monday, 29 August 2005 Washington DC Convention Center -- Hall A, Poster

Division of Chemical Education

The 230th ACS National Meeting, in Washington, DC, Aug 28-Sept 1, 2005