ORGN 336 |
Fluorogenic peptide sequences – transformation of short peptides into fluorophores under ambient photooxidative conditions
| David L. Van Vranken1, Gary L Juskowiak II1, Shawn J. Stachel2, and Parcharee Tivitmahaisoon3. (1) Department of Chemistry, University of California, Irvine, CA 92697, (2) Medicinal Chemistry Department, Merck Research Laboratories, West Point, PA 19486, (3) Roche Bioscience, 3401 Hillview Ave, Palo Alto, CA 94304 |
| Long-lived proteins are susceptible to non-enzymatic chemical reactions and the evolution of fluorescence; however little is known about the sequence-dependence of fluorogenesis. We identified five photooxidative fluorogenic sequences by microsequencing unreacted peptide from fluorescent beads generated by exposing an octapeptide library to light and air. All five of the fluorogenic sequences were ionic; lacked Tyr, His, and Leu; and most of the sequences contained one Trp. Only two of the sequences were fluorogenic as soluble peptides and one of these (H2N-AlaLysProTrpGlyGlyAspAla-CONH2) generated a highly fluorescent photoproduct. The fluorescent photoproduct consisted of a 2-carboxy-quinolin-4-yl moiety fused to the N-terminus of GlyGlyAspAla. This work confirms that peptide photooxidative fluorogenesis is dependent on sequence and not merely on the presence of Trp. Identified fluorogenic sequences could prove to be hot spots for human aging. Also, fluorogenic sequences compatible with intracellular conditions may ultimately serve as fluorescent tags for proteins or as biomaterials. 
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Physical Organic, Combinatorial, Materials, Molecular Recognition
8:00 PM-10:00 PM, Tuesday, March 30, 2004 Anaheim Convention Center -- Hall A, Poster
Division of Organic Chemistry
The 227th ACS National Meeting, Anaheim, CA, March 28-April 1, 2004
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