ORGN 513 |
| Marcey L. Waters and Sarah E. Kiehna. Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599 |
| The binding of carbohydrates by proteins has many biological implications, including recognition of bacterial cell walls, fertilization and viral infection. It has been observed that tryptophan is present in the binding sites of many of these carbohydrate-binding proteins. This is generally attributed to stabilization of the interaction through hydrophobic packing of the sugar against the aromatic side chain or to a carbohydrate-p interaction between the polarized sugar and the aromatic ring of Trp. We have designed a model b-hairpin peptide containing a cross-strand sugar-Trp interaction through the attachment of glucose tetraacetate to the serine side chain and incorporation into the peptide. NOE and chemical shift data indicate an attractive interaction between the glucose and Trp residues. Through a series of thermodynamic and NMR studies relative to control compounds, we are investigating the magnitude and nature of this interaction. |
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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
Sci-Mix
Division of Organic Chemistry |