Site selectivity in self-catalysed functionalization of helical polypeptide structures

Abstract

Histidine side chains in helical structures catalyse the acylation of flanking lysine, ornithine and 1,3-diaminobutyric acid residues provided they are in positions i - 3 and i + 4, but not in positions i - 4, i - 1, i + 2, i + 3, relative to a histidine in position i, in a novel site-selective functionalization reaction that enhances the potential of polypeptide and protein design.