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.
L. Gentilucci, A. Tolomelli, F. Squassabia (2007). Topological exploration of cyclic endomorphin-1 analogues, structurally defined models for investigating the bioactive conformation of MOR agonists. PROTEIN AND PEPTIDE LETTERS, 14, 51-56 [10.2174/092986607779117218].
Topological exploration of cyclic endomorphin-1 analogues, structurally defined models for investigating the bioactive conformation of MOR agonists.
GENTILUCCI, LUCA;TOLOMELLI, ALESSANDRA;SQUASSABIA, FEDERICO
2007
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
