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Synthesis, receptor binding studies, optical spectroscopic and in silico structural characterization of morphiceptin analogs with cis ‐4‐amino‐L‐proline residues
Author(s) -
AdamskaBartłomiejczyk Anna,
Borics Attila,
Tömböly Csaba,
Dvorácskó Szabolcs,
Lisowski Marek,
Kluczyk Alicja,
Wołczański Grzegorz,
PiekielnaCiesielska Justyna,
Janecka Anna
Publication year - 2017
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.3050
Subject(s) - in silico , chemistry , stereochemistry , affinities , amino acid , peptide , proline , binding affinities , amino acid residue , receptor , biochemistry , peptide sequence , gene
Three novel morphiceptin analogs, in which Pro in position 2 and/or 4 was replaced by cis ‐4‐aminoproline connected with the preceding amino acid through the primary amino group, were synthesized. The opioid receptor affinities, functional assay results, enzymatic degradation studies and experimental and in silico structural analysis of such analogs are presented. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.