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J Med Chem. 2012 Nov 26;55(22):10292-6. doi: 10.1021/jm301213s. Epub 2012 Oct 19.

Opioid activity profiles of oversimplified peptides lacking in the protonable N-terminus.

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1
Department of Chemistry "G. Ciamician", University of Bologna, Via Selmi 2, 40126 Bologna, Italy.

Abstract

Recently, we described cyclopeptide opioid agonists containing the d-Trp-Phe sequence. To expand the scope of this atypical pharmacophore, we tested the activity profiles of the linear peptides Ac-Xaa-Phe-Yaa (Xaa = l/d-Trp, d-His/Lys/Arg; Yaa = H, GlyNH(2)). Ac-d-Trp-PheNH(2) appeared to be the minimal binding sequence, while Ac-d-Trp-Phe-GlyNH(2) emerged as the first noncationizable short peptide (partial) agonist with high μ-opioid receptor affinity and selectivity. Conformational analysis suggested that 5 adopts in solution a β-turn conformation.

PMID:
22995061
DOI:
10.1021/jm301213s
[Indexed for MEDLINE]
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