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.
Topological exploration of cyclic endomorphin-1 analogues, structurally defined models for investigating the bioactive conformation of MOR agonists / L. Gentilucci; A. Tolomelli; F. Squassabia. - In: PROTEIN AND PEPTIDE LETTERS. - ISSN 0929-8665. - STAMPA. - 14:(2007), pp. 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.
