Analogues of deltorphin I containing conformationally restricted amino acids in position 2: structure and opioid activity

Autor:	Anika, Lasota, Oliwia, Frączak, Anna, Leśniak, Adriana, Muchowska, Andrzej W, Lipkowski, Michał, Nowakowski, Andrzej, Ejchart, Aleksandra, Olma
Rok vydání:	2014
Předmět:	Male Models Molecular Structure-Activity Relationship Molecular Structure Receptors Opioid delta Receptors Opioid mu Animals Amino Acids Rats Wistar Ligands Oligopeptides Rats
Zdroj:	Journal of peptide science : an official publication of the European Peptide Society. 21(2)
ISSN:	1099-1387
Popis:	New analogues of deltorphin I (DT I, Tyr-D-Ala-Phe-Asp-Val-Val-Gly-NH2 ), with the D-Ala residue in position 2 replaced by α-methyl-β-azido(amino, 1-pyrrolidinyl, 1-piperidinyl or 4-morpholinyl)alanine, were synthesized by a combination of solid-phase and solution methods. All ten new analogues were tested for receptor affinity and selectivity to μ- and δ-opioid receptors. The affinity of analogues containing (R) or (S)-α-methyl-β-azidoalanine in position 2 to δ-receptors strongly depended on the chirality of the α,α-disubstituted residue. Peptide II, containing (S)-α-methyl-β-azidoalanine in position 2, displayed excellent δ-receptor selectivity with its δ-receptor affinity being only three times lower than that of DT I.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::a0469a218f5b776e1ceeeec84e227c52 https://pubmed.ncbi.nlm.nih.gov/25558014 Zobrazit plný text záznamu Plný text