Design of Opioid Peptides for a Potential Delta-Receptor Affinity Label Function: Comparison with the Mu-Specific Tyr-D-Ala-Gly-(Me)Phe- Chloromethyl Ketone

Pharmacology ◽  
1994 ◽  
Vol 49 (2) ◽  
pp. 121-131 ◽  
Author(s):  
A.Z. Rónai ◽  
J. Heρp ◽  
A. Magyar ◽  
A. Borsodi ◽  
K. Medzihradszky
Keyword(s):  
Opioid Peptides ◽  
Chloromethyl Ketone ◽  
Receptor Affinity ◽  
Affinity Label ◽  
Label Function ◽  
Delta Receptor

Synthesis of 3H-Tyr-D-Ala-Gly-N(Me)Phe chloromethyl ketone—an opioid affinity label

Neuropeptides ◽  
1988 ◽  
Vol 12 (3) ◽  
pp. 135-139 ◽  
Author(s):  
E. Varga ◽  
G. Tóth ◽  
J. Hepp ◽  
S. Benyhe ◽  
J. Simon ◽  
...  
Keyword(s):  
Chloromethyl Ketone ◽  
Affinity Label

scholarly journals , -Dimethylphenylalanine : A Useful Aromatic Amino Acid Surrogate for Tyr or Phe Residue in Opioid Peptides

2012 ◽  
Vol 2012 ◽  
pp. 1-11 ◽  
Author(s):  
Yusuke Sasaki ◽  
Akihiro Ambo
Keyword(s):  
Amino Acid ◽  
Opioid Peptides ◽  
Aromatic Amino Acid ◽  
Aromatic Amino Acids ◽  
Hydroxyl Group ◽  
Peptide Mimetics ◽  
Structural Elements ◽  
Receptor Selectivity ◽  
Receptor Affinity ◽  
High Affinity

Two aromatic amino acids, Tyr1 and Phe3 or Phe4, are important structural elements in opioid peptides because they interact with opioid receptors. The usefulness of an artificial amino acid residue ,-dimethylphenylalanine (Dmp) was investigated as an aromatic amino acid surrogate for several opioid peptides, including enkephalin, dermorphin, deltorphin, endomorphin, dynorphin A, and nociceptin peptides. In most peptides, substitutions of Phe3 by a Dmp residue produced analogs with improved receptor-binding affinity and selectivity, while the same substitution of Phe4 induced markedly reduced receptor affinity and selectivity. Interestingly, replacement of Tyr1 by Dmp produced analogs with unexpectedly high affinity or produced only a slight drop in receptor affinity and bioactivity for most peptides. Thus, Dmp is also a useful surrogate for the N-terminal Tyr residue in opioid peptides despite the lack of a phenolic hydroxyl group, which is considered necessary for opioid activity. The Dmp1-substituted analogs are superior to ,-dimethyltyrosine (Dmt)1-substituted analogs for high receptor selectivity since the latter generally have poor receptor selectivity. Thus, Dmp is very useful as an aromatic amino acid surrogate in opioid peptides and may be useful for developing other novel peptide mimetics with high receptor specificity.

Tyr-D-Ala-Gly-(Me)Phe-chloromethyl ketone: A specific affinity label for the opioid receptor

Neuropeptides ◽  
1987 ◽  
Vol 9 (3) ◽  
pp. 225-235 ◽  
Author(s):  
S Benyhe ◽  
J Hepp ◽  
J Simon ◽  
A Borsodi ◽  
K Medzihradszky ◽  
...  
Keyword(s):  
Opioid Receptor ◽  
Chloromethyl Ketone ◽  
Affinity Label ◽  
Specific Affinity

Ketononestrol Aziridine, an Agonistic Estrogen Receptor Affinity Label: Study of Its Bioactivity and Estrogen Receptor Covalent Labeling*

Endocrinology ◽  
1987 ◽  
Vol 121 (2) ◽  
pp. 667-676 ◽  
Author(s):  
JONATHAN F. ELLISTON ◽  
JEFFERY A. ZABLOCKI ◽  
BENITA S. KATZENELLENBOGEN ◽  
JOHN A. KATZENELLENBOGEN
Keyword(s):  
Estrogen Receptor ◽  
Covalent Labeling ◽  
Label Study ◽  
Receptor Affinity ◽  
Affinity Label ◽  
Estrogen Receptor Affinity

o-Naphthalenedicarboxaldehyde Derivative of 7‘-Aminonaltrindole as a Selective δ-Opioid Receptor Affinity Label

2007 ◽  
Vol 50 (14) ◽  
pp. 3392-3396 ◽  
Author(s):  
Sarika Prabhu Haris ◽  
Yan Zhang ◽  
Bertrand Le Bourdonnec ◽  
Christopher R. McCurdy ◽  
Philip S. Portoghese
Keyword(s):  
Opioid Receptor ◽  
Receptor Affinity ◽  
Affinity Label ◽  
Δ Opioid Receptor

DIPPA: An opioid receptor affinity label that produces selective and long-lasting κ antagonism in mice

1994 ◽  
Vol 54 (1) ◽  
pp. 49-50
Author(s):  
An-Chih Chang ◽  
Akira E. Takemori ◽  
Philip S. Portoghese
Keyword(s):  
Opioid Receptor ◽  
Receptor Affinity ◽  
Affinity Label

Alleviation of pain and depression by specific neural transplants: Fine structural correlates

1992 ◽  
Vol 50 (2) ◽  
pp. 1066-1067
Author(s):  
George D. Pappas ◽  
Jacqueline Sagen
Keyword(s):  
Opioid Peptides ◽  
Chromaffin Cells ◽  
Pain Sensitivity ◽  
Opioid Peptide ◽  
Local Source ◽  
Pain Models ◽  
Neural Transplants ◽  
Adrenergic Antagonists ◽  
Csf Levels ◽  
Donor Source

We have been interested in the use of neural transplants mainly as a local source of neuroactive substances, rather than as a replacement for damaged neural circuities. In particular, we have been exploring the possibilities of reducing pain by transplants of opioid peptide producing cells, and reducing depression by transplants of monoamine-producing cells. For the past several years, work in our laboratory has demonstrated in both acute and chronic pain models that transplantation of adrenal medullary tissue or isolated chromaffin cells into CNS pain modulatory regions can reduce pain sensitivity in rodents. Chromaffin cells were chosen as donor source since they produce high levels of both opioid peptides and catecholamines, substances which independently, and probably synergistically, reduce pain sensitivity when injected locally into the spinal cord. The analgesia produced by these transplants most likely results from the release of both opioid peptides and catecholamines, since it can be blocked or attenuated by opiate or adrenergic antagonists, respectively. Furthermore, CSF levels of met-enkephalin and catecholamines are increased by the transplants.

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