Unique conformations of α/β alternating poly(benzyl-glutamate)

PMSE 107

Jianjun Cheng, jianjunc@uiuc.edu, Department of Materials Science and Engineering, University of Illinois at Urbana-Champaign, 201 MSEB, 1304 West Green Street, Urbana, IL 61801 and Timothy J. Deming, demingt@seas.ucla.edu, Departments of Bioengineering and Chemistry and Biochemistry, University of California, Los Angeles, 7523 Boelter Hall, Box 951600, Los Angeles, CA 90095-1600.
Both α- and β-peptides can adopt stable secondary structures in solution. The most common helical conformation of α-peptides is a right-handed 3.6 helix (3.6 residues per turn), while β-peptides containing homologated amino acid residues adopt a left-handed 31 helical conformation (3 residues per turn). Peptides with heterogeneous backbones, composed of alternating α- and β-amino acids, likely adopt well-defined secondary structures as well. Herein we report the design and synthesis of alternating α/β poly(Benzyl-Glutamate). We aim to study their conformations and possible helical senses.
 

Polymers, Nanoparticles and Composite Materials in Nanoscience
1:30 PM-4:50 PM, Monday, 27 March 2006 OMNI at CNN Center -- Intl. Blrm D, Oral

Division of Polymeric Materials: Science and Engineering

The 231st ACS National Meeting, Atlanta, GA, March 26-30, 2006