Download or read book Unnatural Amino Acids Designed for Click Chemistry and Their Application to the Modification of Peptides & Nitrene Transfer Reactions Catalyzed by Metalloporphyrins written by and published by . This book was released on 2009 with total page 223 pages. Available in PDF, EPUB and Kindle. Book excerpt: The field of peptidomimetics has rapidly grown into an area of great interest for the design and synthesis of pharmaceutical drug targets. The large array of natural peptides with biological function as well as the growing understanding of the roles of these peptides in biological events has led to a large interest in these compounds as drug candidates. The majority of peptide and peptide-like molecules have not found widespread pharmaceutical utility; however, due to there lability in biological systems. This major drawback leads to the necessity for the development of peptide-like molecules with increased stability under biological conditions. To this end there has been an increased interest in the development of unnatural amino acids for the synthetic modification of peptides and proteins. Presented in this dissertation is the synthesis of a series of unnatural amino acids designed for applications to [3+2] click cycloaddition reactions. It also covers the introduction of these amino acids into the sequence of peptides for the purpose of labeling the peptide with aryl triazole chromophores in an attempt to analyze the electron transfer capabilities of aryl triazoles. The information from the fluorescent studies of these peptides will provide a basis for the design of fluorophoric peptide probes that can be introduced into a peptide at any time under labile conditions. This methodology provides a powerful tool for the analysis of peptide structure and the analysis of peptide-macromolecular interactions.