Effect of fullerene amino acids with flexible linkage unit on peptide's cell transport and peptide's secondary structure

ORGN 596

Nadjmeh Doostdar, nd4980@rice.edu, Department of Chemistry, Rice University, 6100 Main street, Houston, TX 77005 and Andrew R. Barron, arb@rice.edu, Department of Chemistry, Smalley Institute for Nanoscale Science and Technology, Rice University, 6100 Main Street, Houston, TX 77005.
In previous investigations, we synthesized a series of fullerene amino acids derived from phenylalanine, lysine, and Bucky amino acid (Baa). Our studies showed that phenylalanine based fullerene amino acids are stable under conditions of solid phase peptide synthesis (SPPS) and facilitate the transport of peptides into cell. The phenylalanine provides a rigid spacer between the fullerene and peptide backbone while lysine offers a flexible linkage between the fullerene and peptide chain. In addition, the position of phenylalanine based fullerene within the peptide sequence affects the structure and relative stability of the peptide. Currently, we are investigating the effect of fullerene with lysine linkage unit on peptide's cell transport and also the effect of its position on peptides secondary structures and stability.
 

New Reactions and Methodology, Heterocycles and Aromatics, Bioorganic Chemistry
8:00 PM-10:00 PM, Tuesday, 12 September 2006 Moscone Center -- Hall D, Poster

Sci-Mix
8:00 PM-10:00 PM, Monday, 11 September 2006 Moscone Center -- Hall D, Sci-Mix

Division of Organic Chemistry

The 232nd ACS National Meeting, San Francisco, CA, September 10-14, 2006