The use of the click reaction for the introduction of conjugate groups, such as affinity or fluorescent labels, to a peptide for the study of peptide biochemistry and pharmacology is widespread. However, the nature and location of substituted 1,2,3-triazoles in peptide sequences may markedly affect conformation or binding as compared with native sequences. We have examined the preparation and application of propargyloxyproline (Pop) residues as a precursor to such peptide conjugates. Pop residues are available in a range of regio- and stereoisomers from hydroxyproline precursors and are readily prepared in Fmoc-protected form. They can be incorporated routinely in peptide synthesis, and broadly retain the conformational properties of the parent proline containing peptides.
We report here on the synthesis of a range of Fmoc-protected Pop regio- and stereoisomers and their incorporation into two classes of peptide of interest in our laboratories. The first were derivatives of the Y1 receptor antagonist peptide, BVD15, and the second were cyclic hexapeptides incorporating a Lys–Ile–Asp–Asn pharmacophore motif of lens epithelium-derived growth factor (LEDGF), a key protein for the activity of HIV integrase. This approach to labelling is exemplified by the preparation of biotin- and fluorophore-labelled peptides derived from linear and cyclic peptides.