ORGN 430 |
| Beta-turns are known to be important sites for protein-protein and protein-peptide interactions, but there has been little research exploring the range of functionality that can be incorporated while maintaining a well-folded structure. To probe the effect of amending turn residue side chains, beta-hairpin peptides containing the known type 1' turn sequence Val-Asn-Gly-Orn(Lys) were synthesized with modifications that include alkylation of Asn and acylation of Lys. Analysis by NMR demonstrates that in moderately to well-folded systems these variations impose only a small energetic penalty (<0.5 kcal/mol). These results illustrate the potential that beta-turns possess for covalent modification allowing the display of a wide range of functionality. Specific applications including biotinylation and fluorescent labeling will be discussed. |
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Bioorganic, Metal-Mediated Reactions, and Molecular Recognition
8:00 PM-10:00 PM, Tuesday, 30 August 2005 Washington DC Convention Center -- Hall A, Poster
Sci-Mix
Division of Organic Chemistry |