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.
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Calderan, A., Ruzza, P., Ancona, B. et al. Synthesis, conformational and pharmacological studies on dermorphin N-terminal tetrapeptide analogues. Letters in Peptide Science 5, 71–73 (1998). https://doi.org/10.1023/A:1008805431117
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DOI: https://doi.org/10.1023/A:1008805431117