Polythiazole linkers as functional rigid connectors: a new RGD cyclopeptide with enhanced integrin selectivityElectronic supplementary information (ESI) available. See DOI: 10.1039/c4sc00572d

Polythiazole amino acids clasp linear peptides to generate cyclic derivatives, however, the resulting species are not merely stapled peptides but bear a complex heterocyclic moiety displaying its intrinsic set of interactions. As a proof of concept, a bisthiazole moiety has been grafted onto an RGD sequence to deliver a new cilengitide analogue with improved integrin selectivity and remarkable in vivo antiangiogenic activity. Polythiazole amino acids clasp linear peptides to generate cyclic derivatives, however, the resulting species are not merely stapled peptides but bear a complex heterocyclic moiety displaying its intrinsic set of interactions.