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Wyszukujesz frazę "cyclic opioid peptides" wg kryterium: Temat

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    Wyświetlanie 1-2 z 2
    Tytuł:
    Cyclic enkephalin-deltorphin hybrids containing a carbonyl bridge: structure and opioid activity
    Autorzy:
    Ciszewska, Małgorzata
    Ruszczyńska, Katarzyna
    Oleszczuk, Marta
    Chung, Nga
    Witkowska, Ewa
    Schiller, Peter
    Wójcik, Jacek
    Izdebski, Jan
    Powiązania:
    https://bibliotekanauki.pl/articles/1039922.pdf
    Data publikacji:
    2011
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    cyclic opioid peptides
    conformation
    NMR
    N-(ureidoethyl)amides
    side-chain to side-chain cyclization
    structure-activity relationship
    Opis:
    Six hybrid N-ureidoethylamides of octapeptides in which an N-terminal cyclic structure related to enkephalin was elongated by a C-terminal fragment of deltorphin were synthesized on MBHA resin. The synthetic procedure involved deprotection of Boc groups with HCl/dioxane and cleavage of the peptide resin with 45 % TFA in DCM. d-Lys and d-Orn were incorporated in position 2, and Lys, Orn, Dab, or Dap in position 5. The side chains of the dibasic amino function were protected with the Fmoc group. This protection was removed by treatment with 55 % piperidine in DMF, and cyclization was achieved by treatment with bis-(4-nitrophenyl)carbonate. Using various combinations of dibasic amino acids, peptides containing a 17-, 18-, 19- or 20-membered ring structure were obtained. The peptides were tested in the guinea-pig ileum (GPI) and mouse vas deferens (MVD) assays. Diverse opioid activities were observed, depending on the size of the ring. Extension of the enkephalin sequence at the C-terminus by a deltorphin fragment resulted in a change of receptor selectivity in favor of the δ receptor. The conformational propensities of selected peptides were determined using the EDMC method in conjunction with data derived from NMR experiments carried out in water. This approach allowed proper examination of the dynamical behavior of these small peptides. The results were compared with those obtained earlier with corresponding N-(ureidoethyl)pentapeptide amides.
    Źródło:
    Acta Biochimica Polonica; 2011, 58, 2; 225-230
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Cyclic dermorphin tetrapeptide analogues obtained via ring-closing metathesis
    Autorzy:
    Berezowska, Irena
    Chung, Nga
    Lemieux, Carole
    Wilkes, Brian
    Schiller, Peter
    Powiązania:
    https://bibliotekanauki.pl/articles/1041269.pdf
    Data publikacji:
    2006
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    opioid activity profile in vitro
    cyclic dermorphin analogues
    opioid peptides
    ring-closing metathesis
    dermorphin
    Opis:
    The dermorphin-derived cyclic tetrapeptide analogues H-Tyr-c[d-Cys-Phe-Cys]NH2 and H-Tyr-c[d-Cys-Phe-D-Cys]NH2 are opioid agonists at the µ and δ receptor. To enhance the metabolic stability of these peptides, we replaced the disulfide bridge with a bis-methylene moiety. This was achieved by solid-phase synthesis of the linear precursor peptide containing allylglycine residues in place of the Cys residues, followed by ring-closing metathesis. In the case of the peptide with L-configuration in the 4-position both the cis and the trans isomer of the resulting olefinic peptides were formed, whereas the cis isomer only was obtained with the peptide having the d-configuration in position 4. Catalytic hydrogenation yielded the saturated -CH2-CH2- bridged peptides. In comparison with the cystine-containing parent peptides, all olefinic peptides showed significantly reduced µ and δ agonist potencies in the guinea pig ileum and mouse vas deferens assays. The -CH2-CH2-bridged peptide with l-configuration in the 4-position was equipotent with its cystine-containing parent in both assays, whereas the bis-methylene analogue with d-configuration in position 4 was 10-27-fold less potent compared to its parent. The effect of the disulfide replacements with the -CH=CH- and-CH2-CH2- moieties on the conformational behavior of these peptides was examined by theoretical conformational analysis which provided plausible explanations in terms of structural parameters for the observed changes in opioid activity.
    Źródło:
    Acta Biochimica Polonica; 2006, 53, 1; 73-76
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-2 z 2

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