title: Topological exploration of cyclic endomorphin-1 analogues, structurally defined models for investigating the bioactive conformation of MOR agonists.
abstract: Although there have been several reports on the conformational analysis of endomorphin-1 (YPWF-NH(2)) and related MOR (mu-opioid receptor) agonists, a definitive, convincing model of the biologically active structure is not yet available. We recently reported the synthesis and pharmacological characterization of the atypical endomorphin-analogue agonist c[YpwFG]. In this paper we discuss the conformational analysis of c[YpwFG] in comparison to its epimers, for investigating the topological features responsible for ligand recognition and receptor activation, and the role of the different pharmacophores.
authors.affiliation: Dipartimento di Chimica G. Ciamician, via Selmi 2, Università degli Studi di Bologna, 40126 Bologna, Italy. luca.gentilucci@unibo.it
authors.forename: Luca
authors.initials: L
authors.lastname: Gentilucci
authors.forename: Alessandra
authors.initials: A
authors.lastname: Tolomelli
authors.forename: Federico
authors.initials: F
authors.lastname: Squassabia
mesh_terms: D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry*; D018847:Opioid Peptides / Q000737:chemistry* / Q000494:pharmacology*; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000494:pharmacology*; D017433:Protein Structure, Secondary; D017450:Receptors, Opioid, mu / Q000819:agonists*; D013329:Structure-Activity Relationship
chemical_list: D009842:Oligopeptides; D018847:Opioid Peptides; D010456:Peptides, Cyclic; D017450:Receptors, Opioid, mu; C105293:endomorphin 1