scholarly journals Synthesis and binding properties of deltorphin I analogues containing (R) and (S)-alpha-hydroxymethylnaphtylalanine.

2001 ◽  
Vol 48 (4) ◽  
pp. 1165-1168 ◽  
Author(s):  
A Olma ◽  
A Gniadzik ◽  
A W Lipkowski ◽  
M Lachwa
Keyword(s):  
Amino Acid ◽  
Opioid Receptor ◽  
Delta Opioid Receptor ◽  
Binding Properties ◽  
Lower Affinity ◽  
Receptor Affinity ◽  
Amino Acid Enantiomers ◽  
Phenylalanine Residue ◽  
Delta Receptors ◽  
Disubstituted Amino Acid

New analogues of deltorphin I (DT I), in which the phenylalanine residue in position 3 is substituted with amphiphilic alpha,alpha-disubstituted amino acid enantiomers, (R) and (S)-alpha-hydroxymethylnaphtylalanine, were synthesized and tested for mu and delta opioid receptor affinity and selectivity. Although both analogues have lower affinity to delta receptors than DT I, they both expressed specificity to delta receptors.

scholarly journals β2-Homo-Amino Acid Scan of µ-Selective Opioid Tetrapeptide TAPP

Molecules ◽  
2020 ◽  
Vol 25 (10) ◽  
pp. 2461 ◽  
Author(s):  
Dagmara Tymecka ◽  
Piotr F. J. Lipiński ◽  
Piotr Kosson ◽  
Aleksandra Misicka
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Human Plasma ◽  
Opioid Receptor ◽  
Molecular Modelling ◽  
Parent Compound ◽  
Common Element ◽  
Ionic Interaction ◽  
Receptor Affinity ◽  
Δ Opioid Receptor

TAPP (H-Tyr-d-Ala-Phe-Phe-NH2) is a potent, µ-selective opioid ligand. In order to gain further insights into pharmacophoric features of this tetrapeptide, we have performed a β2-Homo-amino acid (β2hAA) scan of the TAPP sequence. To this aim, 10 novel analogues have been synthesized and evaluated for µ-opioid and δ-opioid receptor affinity as well as for stability in human plasma. The derivatives included compounds in which a (R)- or (S)-β2-Homo-Homologue replaced the amino acids in the TAPP sequence. The derivatives with (R)- or (S)-β2hPhe4 turned out to bind µOR with affinities equal to that of the parent. β2hAAs in position 1 and 3 resulted in rather large affinity decreases, but the change differed depending on the stereochemistry. β2-Homologation in the second position gave derivatives with very poor µOR binding. According to molecular modelling, the presented α/β-peptides adopt a variety of binding poses with their common element being an ionic interaction between a protonable amine of the first residue and Asp147. A feature required for high µOR affinity seems the ability to accommodate the ring in the fourth residue in a manner similar to that found for TAPP. Contrary to what might be expected, several compounds were significantly less stable in human plasma than the parent compound.

scholarly journals Identification of a Critical Amino Acid Position Conferring G‐protein Bias to Delta Opioid Receptor Peptides

2019 ◽  
Vol 33 (S1) ◽  
Author(s):  
Robert Cassell ◽  
Breanna Zerfas ◽  
Benjamin Cummins ◽  
Darci Trader ◽  
Richard Rijn
Keyword(s):  
Amino Acid ◽  
G Protein ◽  
Opioid Receptor ◽  
Amino Acid Position ◽  
Delta Opioid Receptor ◽  
Critical Amino Acid

Topographical conformations of the deltorphins predicate .delta. opioid receptor affinity

1993 ◽  
Vol 115 (18) ◽  
pp. 8503-8504 ◽  
Author(s):  
Sharon D. Bryant ◽  
Severo Salvadori ◽  
Martti Attila ◽  
Lawrence H. Lazarus
Keyword(s):  
Opioid Receptor ◽  
Delta Opioid Receptor ◽  
Receptor Affinity

Levels of Delta-Opioid Receptor mRNA in Morphine-Tolerant Mice

Analgesia ◽  
1995 ◽  
Vol 1 (3) ◽  
pp. 195-200 ◽  
Author(s):  
Benjamin Kest ◽  
Shirzad Jenab ◽  
Charles E. Inturrisi
Keyword(s):  
Opioid Receptor ◽  
Delta Opioid Receptor ◽  
Receptor Mrna
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