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Synthesis and biological activity profile of new analogues of the cyclic opioid peptide H‐Tyr‐c[ D ‐Cys‐Gly‐Phe( p NO 2 )‐ D ‐Cys]‐NH 2 containing ( S )‐α‐hydroxymethylcysteine in place of cysteine
Author(s) -
Witkowska Renata,
Chung Nga N.,
Schiller Peter W.,
Zabrocki Janusz
Publication year - 2005
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.620
Subject(s) - chemistry , peptide , stereochemistry , biological activity , residue (chemistry) , agonist , opioid peptide , receptor , cyclic peptide , opioid , peptide synthesis , biochemistry , in vitro
To examine the effect on biological activity of replacing D ‐Cys in the opioid peptide H‐Tyr‐c[ D ‐Cys‐Gly‐Phe( p NO 2 )‐ D ‐Cys]‐NH 2 in position 2 or/and 5 with α‐hydroxymethylcysteine (α‐Hmc), three analogues were synthesized. These compounds exhibit agonist activity at both µ and δ receptors. However, the most active analogue, with ( S )‐α‐Hmc residue in position 5, was 3360‐ and 2190‐fold less active than the parent peptide in the GPI and MVD assays, respectively. Copyright © 2004 European Peptide Society and John Wiley & Sons, Ltd.