Dermorphin structure-activity relationships toward μ and δ opioid receptors were investigated using a series of synthetic peptides, in which the aromatic residues at positions 1 or/and 3 of the N-terminal tetrapeptide analogue H-Tyr-D-Arg-Phe-β-Ala-NH2 were replaced by unnatural or constrained amino acids.
Synthesis, conformational and pharmacological studies on dermorphin N-terminal tetrapeptide analogues
CIMA, LORENZO;GIUSTI, PIETRO;
1998
Abstract
Dermorphin structure-activity relationships toward μ and δ opioid receptors were investigated using a series of synthetic peptides, in which the aromatic residues at positions 1 or/and 3 of the N-terminal tetrapeptide analogue H-Tyr-D-Arg-Phe-β-Ala-NH2 were replaced by unnatural or constrained amino acids.File in questo prodotto:
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