CHED 852 |
| Nicholas J. Slodki, Division of Natural Science and Mathematics, Division of Natural Science and Mathematics, Transylvania University, 300 North Broadway, Lexington, KY 40508 |
| Spermine analogues have been shown to inhibit N-arginine dibasic convertase, an enzyme that cleaves various physiological peptides. For one particular derivative, of 1N,16N-bis(trifluoroacetyl)-7N-4-nitrobenzyl spermine, previous work using proton magnetic resonsance characterization showed somewhat appreciable reduction of the aromatic nitro group using a zinc metal with acid catalyst. While the results were favorable, purification and yield were not. Thus, a new reduction scheme using tin and acid catalyst was achieved with 4-nitrobenzyl bromide, the aromatic constituent that has been internally substituted onto protected spermine in pervious work. Reactions carried out using the aforementioned technique and varying the strength of extraction base during purification has given yields >75% for 4-aminobenzyl bromide. Therefore, the same technique has been attempted for 1N,16N-bis(trifluoroacetyl)-7N-4-nitrobenzyl spermine, giving yields just at 50%. Subsequent deprotection with base yielded the analogue, in higher yield and purity. |
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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 |