Cenderitide: a multivalent designer-peptide-agonist of particulate guanylyl cyclase receptors with considerable therapeutic potential in cardiorenal disease states

Abstract

This editorial refers to ‘Cenderitide: structural requirements for the creation of a novel dual particulate guanylyl cyclase receptor agonist with renal-enhancing in vivo and ex vivo actions’, by C.Y.W. Lee et al ., doi:10.1093/ehjcvp/pvv040. In their article, Lee et al. describe and structurally analyse renal effects of a novel chimeric designer peptide that activates two particulate guanylyl cyclase receptors.1 This designer peptide named cenderitide, which is currently tested in clinical trials for heart failure, consists of the 5 amino acid amino-terminus and the 17 amino acid disulphide ring of C-type natriuretic peptide (CNP) to which the 15 amino acid carboxylterminus of Dendroaspis NP (DNP) was fused.2–4 DNP is a natriuretic peptide isolated from the venom of the eastern green mamba snake ( Dendroaspis agusticeps ).1,2 CNP is considered to be the phyologenetically oldest member of the family of natriuretic peptides, which, contrary to …