Beta-hairpin peptides that fold due to fluoroaromatic contacts

ORGN 774

Chihui An, ahamindra@berkeley.edu, Tsz Na Ko, ahamindra@berkeley.edu, and Ahamindra Jain, ahamindra@berkeley.edu. Department of Chemistry, University of California, Berkeley, 332 Latimer Hall, Mail Code 1460, Berkeley, CA 94720-1460
12-mer peptides including the epitope found in the V3 loop of GP120, a glycoprotein found in the envelope of HIV virus have been prepared. These structures include a pentafluorophenylalanine residue, which we believe should encourage the folding of the peptides due to ion-quadrupole or quadrupole-quadrupole interactions. Evidence for formation of specific structures from 1- and 2-D NMR spectroscopy will be presented.
 

Total Synthesis, Materials, Molecular Recognition, Process R&D, and Physical Organic Chemistry
8:00 PM-10:00 PM, Wednesday, 13 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