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Wyszukujesz frazę "molecular receptors" wg kryterium: Temat

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    Wyświetlanie 1-5 z 5
    Tytuł:
    Cellulose as a matrix for synthesis of the library of molecular receptors useful for screening of antihistamine compounds
    Autorzy:
    Walczak, M. E.
    Fraczyk, J.
    Kaminski, Z. J.
    Kolesinska, B.
    Powiązania:
    https://bibliotekanauki.pl/articles/285804.pdf
    Data publikacji:
    2017
    Wydawca:
    Akademia Górniczo-Hutnicza im. Stanisława Staszica w Krakowie. Polskie Towarzystwo Biominerałów
    Tematy:
    biopolymers
    antihistamine compounds
    molecular receptors
    Źródło:
    Engineering of Biomaterials; 2017, 20, no. 143 spec. iss.; 50
    1429-7248
    Pojawia się w:
    Engineering of Biomaterials
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Functionalized cellulose as a matrix for the synthesis of library of molecular receptors useful for screening of compounds with anti-histamine activity
    Autorzy:
    Walczak, M. E.
    Frączyk, J.
    Kamiński, Z. J.
    Kolesińska, B.
    Powiązania:
    https://bibliotekanauki.pl/articles/285956.pdf
    Data publikacji:
    2017
    Wydawca:
    Akademia Górniczo-Hutnicza im. Stanisława Staszica w Krakowie. Polskie Towarzystwo Biominerałów
    Tematy:
    molecular receptors
    immobilized peptides
    binding pocket
    agonist/antagonist
    histamine receptors
    Opis:
    The library of molecular receptors was formed by self-organization of N-heptanoylated dipeptides anchored in the regular fashion via aminophenylamino- 1,3,5-triazine linker to the surface of cellulose membrane. SPOT method was used for the synthesis of peptide library. As C-terminal amino acids of peptide fragments were attached: Ala, Pro and Phe, while as a N-terminal amino acids were applied all natural amino acids. DMT/NMM/TosO- was selected as a coupling reagent for synthesis of library of N-heptanoylated dipeptides. These constructs were used as a tool for distinguishing pharmaceutically active compounds acting on histamine receptors. In the studies as active compounds were tested: Doxylamine and Difenhydramine with histamine agonist activity, Ranitidine and Cimetidine with antagonist activity as well as Histamine – natural ligand. The binding of colourless ligands was monitored by staining with Brilliant Black used as reporter dye and quantitative colour measurement was performed in 256 grade gray scale by using Image-Quant software. Substantial differences in the ability of interactions of agonists and antagonists with bounding pockets were observed with selected molecular receptors. From 60 elements library of molecular receptors were selected 12, which were able to distinguish between agonists or antagonists. It has been found that even small changes (Leu residue vs Val residue) in the structure of molecular receptor influenced specificity of agonist or antagonist binding.
    Źródło:
    Engineering of Biomaterials; 2017, 20, 142; 2-6
    1429-7248
    Pojawia się w:
    Engineering of Biomaterials
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Signal transmission via G protein-coupled receptors in the light of rhodopsin structure determination.
    Autorzy:
    Ciarkowski, Jerzy
    Drabik, Piotr
    Giełdoń, Artur
    Kaźmierkiewicz, Rajmund
    Ślusarz, Rafał
    Powiązania:
    https://bibliotekanauki.pl/articles/1044085.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    signal transduction
    neurohypophyseal receptors
    molecular modeling
    GPCRs
    Opis:
    G protein-coupled receptors (GPCRs) transducing diverse external signals to cells via activation of heterotrimeric GTP-binding (G) proteins, estimated to mediate actions of 60% of drugs, had been resistant to structure determination until summer 2000. The first atomic-resolution experimental structure of a GPCR, that of dark (inactive) rhodopsin, thus provides a trustworthy 3D prototype for antagonist-bound forms of this huge family of proteins. In this work, our former theoretical GPCR models are evaluated against the new experimental template. Subsequently, a working hypothesis regarding the signal transduction mechanism by GPCRs is presented.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 4; 1203-1207
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Preliminary studies of interaction between nanotubes and toll-like receptors
    Autorzy:
    Mozolewska, M. A.
    Krupa, P.
    Rasulev, B.
    Liwo, A.
    Leszczyński, J.
    Powiązania:
    https://bibliotekanauki.pl/articles/1935817.pdf
    Data publikacji:
    2014
    Wydawca:
    Politechnika Gdańska
    Tematy:
    CNTs
    toll-like receptors
    molecular dynamics
    receptory toll-like
    dynamika molekularna
    Opis:
    Toll-like receptors ( TLR s) are a group of proteins which play a crucial role in the innate immune system. The main function of TLR s is to recognize structurally conserved molecules, which are inserted to the organism of the host by microbes, and then to activate the immune response. Current development of drugs is often connected not only with the drug itself, but also with the way it is delivered into the human body to interact direc tly with the source of the problem. Carbon nanostructures, particularly nanotubes, are one of the car rier molecules of the future. However, there is still no knowledge about the exact mechani sms of toxicity and possible interactions with macromolecules, such as proteins. In our study we tr ied to determine, if the nanotubes could interfere with the innate immune system by interac ting with TLR s. For this purpose, we used the following TLR structures downloaded from the RCSB Protein Data Bank: TLR 2 (3 A 7 C ), TLR 4/ MD (3 FXI ), TLR 5 (3 V 47), TLR 3 (2 A 0 Z ), and the complexes of TLR 1/ TLR 2 (2 Z 7 X ) and TLR 2/ TLR 6 (3 A 79). The preliminary results of our Steered Molecular Dynamics ( SMD ) simulations have shown that nanotubes interact very strongly with the binding pockets of some receptors ( e.g. TLR 2), which results in their binding to these sites without subst antial use of the external force.
    Źródło:
    TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk; 2014, 18, 4; 351--355
    1428-6394
    Pojawia się w:
    TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Investigation of interactions between dermorphin analogs and µ-opioid receptor
    Autorzy:
    Karczyńska, A.
    Zaborowski, B.
    Ślusarz, M.
    Powiązania:
    https://bibliotekanauki.pl/articles/1935820.pdf
    Data publikacji:
    2014
    Wydawca:
    Politechnika Gdańska
    Tematy:
    molecular modeling
    opioid receptors
    defmorphin
    molecular docking
    drug design
    modelowanie molekularne
    receptory opioidowe
    dokująca molekularna
    projektowanie leków
    dermorfina
    Opis:
    Opioid receptors play the pain control function in the body. Most of the research is carried out to find the most effective analgesic. The earliest analgesic is morphine, however, unfortunately it has many side effects [Mizoguchi H et al. 2003 J. Pharmacol Sci. 93 423]. At a later time dermorphin was discovered as another potent analgesic [Mont ecucchi P C et al. 1981 Int. J. Pept. Protein Res. 17 275]. Unfortunately, this peptide is not resistant to enzymatic metabolism [Kisara K et al. 1986 Br. J. Pharmacol. 87 183; Sasaki Y et al. 1985 Neuropeptides 5 391]. The objective of this study is to search for new opioid analgesics by investigation of interactions between dermorphin analogs and the μ -opioid receptor using molecular modeling methods. MOPR ( μ -Opioid Peptide Receptor) complexes with several ligands (with known biological activity) were modeled to explain how the structure of the complex was related to the biological activity. The investigated dermorphin analogs containing [ DMT1, D -Arg 2 ] (especially tetrapeptides) may become a good alternative for the currently used an algesics.
    Źródło:
    TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk; 2014, 18, 4; 331--336
    1428-6394
    Pojawia się w:
    TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-5 z 5

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