ORGN 528 |
A general approach for the stabilization of peptide secondary structures
| Gianluca Dimartino, Ross Chapman, Nicholas G. Angelo, and Paramjit S. Arora. Department of Chemistry, New York University, 100 Washington Sq East, New York, NY 10003 |
We have initiated a research program to develop new approaches for the stabilization of desired secondary structures (a-helix, 310-helix, p-helix, or b-turn) in small peptides. Although several methods for constraining peptides in a-helix and b-turn conformations have been reported, in these approaches the constraining templates typically block or replace important solvent-exposed surfaces in the designed peptidomimetics. The choice and the placement of constraining elements may hamper the use of these peptidomimetics as tools in molecular biology. This poster will present our ongoing work to prepare internally constrained peptides, through an olefin metathesis-based hydrogen bond surrogate approach, that faithfully mimic the three-dimensional structure of a naturally folded peptide. Our methodology may also be extended to access peptide secondary structures not commonly observed in nature. |
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Bioorganic, Molecular Recognition, Asymmetric Reactions and Syntheses
11:00 AM-1:00 PM, Wednesday, September 10, 2003 Javits Convention Center -- Hall 1B/1C, Poster
Division of Organic Chemistry
The 226th ACS National Meeting, New York, NY, September 7-11, 2003
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