Allylglycine-containing peptides may be cleaved selectively at the amide bond between allylglycine and the subsequent amino acid with iodine. The lateral double bond allows selective modifications of a peptide e.g. via metathesis. Replacing cysteine residues by allylglycine allows to obtain carba-analogs of disulfide-bridged peptides.
Educt for obtaining Fmoc-prenylglycine.