Synthesis of highly fluorescent GFP-chromophore analogs

ORGN 393

Liangxing Wu, lwu@mail.chem.tamu.edu, Chemistry, Texas A&M University, 3225 TAMU Chemistry, College Station, TX 77843 and Kevin Burgess, burgess@tamu.edu, Department of Chemistry, Texas A & M University, Box 30012, College Station, TX 77842-3012.
Green fluorescent protein (GFP) from the jellyfish Aeqorea victoria has been extensively studied and become a widely used marker in molecular biology and biochemistry due to its strong intrinsic fluorescence. The chromophore of GFP is a p-hydroxybenzylidene-imidazolidinone derivative formed by autocatalytic, posttranslational cyclization and oxidation of the polypeptide backbone. Unfortunately, the chromophore will totally lose its fluorescence when isolated from the protein. Many GFP-chromophore derivatives have been reported in literature. However, none of those is highly fluorescent. We have synthesized series of GFP-chromophore analogs, which are strongly fluorescent and have similar photophysical properties as GFP. These derivatives were easily functionalized to increase water-solubility. Handles for coupling with biomolecules can also be installed for applications in labeling. The properties of these GFP-chromophore analogs were studied in solution and the application in labeling of biomolecules was also demonstrated.
 

Heterocycles and Aromatics, Molecular Recognition and Self Assembly
8:00 PM-10:00 PM, Tuesday, April 8, 2008 Morial Convention Center -- Hall A, Poster

Division of Organic Chemistry

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008