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Show DETERMINATION OF INTRAMOLECULAR INTERACTIONS WITHIN PEPTIDE CHAINS THROUGH THE USE OF PHOSPHORYLATED AMINO ACIDS Matthew Weinstock (Bruce Yu) Deptartment of Pharmaceutics and Pharmaceutical Chemistry The purpose of this project is to expand current knowledge of peptide chain behaviors, which is important to future advancements in drug delivery docking devices involving peptide molecules. In this project, several different model peptide molecules were synthesized using the Fmoc Solid Phase Peptide Synthesis technique. Each of these peptides, which were typically 14 amino acids long, contained one phosphorylated amino acid at a specific point in the acid sequence of the chain. Once the peptides were purified through HPLC, 31P - NMR spectroscopy could be done on the molecules to determine the pKa of the incorporated phosphate groups. From this pKa value, inferences can be made as to the nature of certain intramolecular interactions within the peptide molecule. This understanding of intramolecular interactions within a peptide molecule is crucial to future developments in peptide related drug delivery. Future projects include taking florescence measurements on peptides which have Tyrosine and Tryptophan incorporated into the peptide chain in order to learn even more about intramolecular interactions. formyl-GpSPPPDPPPDPPPG-amide a model peptide with a phosphorylated amino acid incorperated into the chain Matthew Weinstock Dept. of Pharmaceutics and Pharmaceutical Chemistry Faculty Sponsor Bruce Yu |