TY - JOUR
T1 - Synthesis of enkephalin-based affinity labels for delta opioid receptors
AU - Maeda, DY
AU - Murray, TF
AU - Roth, JE
AU - Aldrich, JV
N1 - Funding Information:
The authorsw ishto thankD r. David G. Grandyf or his generoudso nationo f CHO cellse xpressintgh ed eltar eceptora,n da cknowledgteh eN ationaSl cienceF oundation and an AmericanC hemicaSl ocietyp re-doctorafel llowship(D YM) for financial support.
PY - 1994/11/10
Y1 - 1994/11/10
N2 - Affinity labels (irreversible ligands) are useful pharmacological tools to study receptor structure and function. As part of a program to prepare affinity labels based on opioid peptides, we developed a general synthetic strategy to introduce different electrophilic labeling moieties (i.e. isothiocyanate and bromoacetamide) via a p-amino functionality on a phenylalanine residue. The affinity labelling groups were incorporated into the Phe4 position of the delta opioid receptor antagonists ICI-174,864 (1) and N,N-dibenzyl leucine enkephalin (2). Using an orthogonal Boc/Fmoc protection strategy, the common peptide precursors were assembled in solution, the affinity labels introduced and the peptides deprotected. In cloned δ receptors expressed in CHO cells (3), only the isothiocyanate derivative of N,N-dibenzyl leucine enkephalin exhibited wash-resistant inhibition of [3H]DPDPE binding.
AB - Affinity labels (irreversible ligands) are useful pharmacological tools to study receptor structure and function. As part of a program to prepare affinity labels based on opioid peptides, we developed a general synthetic strategy to introduce different electrophilic labeling moieties (i.e. isothiocyanate and bromoacetamide) via a p-amino functionality on a phenylalanine residue. The affinity labelling groups were incorporated into the Phe4 position of the delta opioid receptor antagonists ICI-174,864 (1) and N,N-dibenzyl leucine enkephalin (2). Using an orthogonal Boc/Fmoc protection strategy, the common peptide precursors were assembled in solution, the affinity labels introduced and the peptides deprotected. In cloned δ receptors expressed in CHO cells (3), only the isothiocyanate derivative of N,N-dibenzyl leucine enkephalin exhibited wash-resistant inhibition of [3H]DPDPE binding.
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U2 - 10.1016/0167-0115(94)90445-6
DO - 10.1016/0167-0115(94)90445-6
M3 - Article
AN - SCOPUS:0028099973
VL - 54
SP - 171
EP - 172
JO - Regulatory Peptides
JF - Regulatory Peptides
SN - 0167-0115
IS - 1
ER -