Investigation of peptide interactions using a synthetic fluorescent amino acid

CHED 594

Allison Perez, aperez@wellesley.edu, Leslie G. Oesterich, loesteri@wellesley.edu, and David R. Haines, DHaines@Wellesley.edu. Department of Chemistry, Wellesley College, 21 Wellesley College Rd., Unit 5239, Wellesley, MA 02481
(S)-2-Amino-3-(7-methoxy-4-coumaryl)-propanoic acid (1), a coumarin-based amino acid, has been prepared to aid the investigation of peptide solution interactions as well as binding affinities of peptide ligands to their corresponding receptors. One particular protein-receptor of interest within the field of diabetes type 2 research is GLP-1 and its receptor GLP-1R. Binding affinity to GLP-1R system is most often determined by competition with radioactive Exendin-4. Several species have been found that activate GLP-1R, but which do not show detectable binding in competition with the very strongly binding Exendin-4. The fluorescent amino acid, upon incorporation into the peptide of interest, will allow for detection of low-level binding in noncompetitive environments via observation of fluorescent emission. The synthesis of the fluorescent amino acid (1), as well as its incorporation into test peptides will be discussed.