Conserved delta-activity in reverse enantiomeric opioid peptide.
A reverse enantiomeric peptide has a reversed amino acid sequence with enantiomeric amino acid residues compared with its parent peptide. In most cases the random change of amino acid sequence or chirality might be expected to bring about significant changes in peptide activity. However, the reverse enantiomeric peptides of Leu-enkephalin and Tyr-D-Ala-Gly-Phe-D-Leu (DADLE) have shown affinity for the opioid delta-receptor, but not for mu- or kappa-receptors. This suggests that delta-opioid receptor recognition occurs primarily through interaction with the peptide side chains, since the native opioid peptide and its reverse enantiomer are able to have similar side-chain conformation.
Doi
M
M
Osaka University of Pharmaceutical Sciences, Japan.
Ishibe
A
A
Shinozaki
H
H
Murata
T
T
Inoue
M
M
Yasuda
M
M
Ishida
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001667:Binding, Competitive; D004743:Enkephalin, Leucine / Q000494:pharmacology; D016308:Enkephalin, Leucine-2-Alanine / Q000494:pharmacology; D006168:Guinea Pigs; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D018847:Opioid Peptides / Q000378:metabolism / Q000494:pharmacology*; D011487:Protein Conformation; D011817:Rabbits; D017465:Receptors, Opioid, delta / Q000187:drug effects* / Q000378:metabolism; D013329:Structure-Activity Relationship
D018847:Opioid Peptides; D017465:Receptors, Opioid, delta; D004743:Enkephalin, Leucine; D016308:Enkephalin, Leucine-2-Alanine