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Topological Exploration of Cyclic Endomorphin-1 Analogues, Structurally Defined Models for Investigating the Bioactive Conformation of MOR Agonists

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Although there have been several reports on the conformational analysis of endomorphin-1 (YPWF-NH2) and related MOR (μ-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.

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Keywords: Cyclic endomorphins; MORs; agonism; bioactive conformation; lipophilic peptides

Document Type: Research Article

Affiliations: Dipartimento di Chimica “G. Ciamician”, via Selmi 2, Universit√† degli Studi di Bologna, 40126 - Bologna, Italy.

Publication date: 2007-01-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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