CHED 804 |
| Laura Edgington, Rebecca Ford, and Eva Csuhai. Division of Natural Sciences and Mathematics, Transylvania University, 300 North Broadway, Lexington, KY 40508 |
| Spermine binding and inhibition of the peptidase nardilysin seems to require the presence of free primary amino groups on the polyamine. In order to elucidate the biological function of spermine and bound nardilysin, a tracking mechanism would be helpful. During this project we add a fluorescent dansyl to one of the secondary amine positions of the molecule in order to determine whether or not such an addition will alter the function of spermine as a nardilysin inhibitor. Electrophiles like dansyl chloride have a preference for the primary ends of spermine. In order to avoid this reaction the primary amines are protected with trifluoroacetyl moieties. After the addition of dansyl chloride, the trifluoroacetyl protecting groups are removed by hydrolysis in base. The fluorescent secondary dansyl-spermine derivative is purified by column chromatography and characterized. The binding of dansyl spermine to nardilysin is characterized by comparing its inhibitory characteristics to those of spermine. |
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Undergraduate Research Poster Session: Organic Chemistry
2:00 PM-4:00 PM, Monday, March 29, 2004 Anaheim Convention Center -- Hall A, Poster
Division of Chemical Education |