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    Wyświetlanie 1-2 z 2
    Tytuł:
    The search for new biological activities for selected insect peptides
    Autorzy:
    Kuczer, M.
    Dziubasik, K.
    Luczak, M.
    Majewska, A.
    Kamysz, W.
    Saniewska, A.
    Konopinska, D.
    Powiązania:
    https://bibliotekanauki.pl/articles/55140.pdf
    Data publikacji:
    2008
    Wydawca:
    Sieć Badawcza Łukasiewicz - Instytut Przemysłu Organicznego
    Tematy:
    antitumour peptide
    antifungal activity
    antiviral peptide
    oostatic peptide
    antiviral activity
    Phoma narcissi
    Botrytis tulipae
    colony growth
    biological property
    antimicrobial activity
    insect peptide
    biological activity
    insect
    peptide
    Opis:
    New biological properties of selected insect peptides are presented. The subjects of the investigation included insect oostatic peptides, like Neb-colloostatin (I) and Neb-TMOF(II), and/or insect peptides with antiviral or antitumor activity, such as alloferon (III) and its analogues modified at position 1 of the peptide chain. In the study was also included the oligopeptide Any-GS (VII) and its truncated analogues. The peptides were tested for antimicrobial activity on a series of bacterial species, antiviral activity against Human Herpes Virus type 1 (HHV-1) in vitro using a Vero cell line, and the growth and development of plant pathogens Phoma narcissi and Botrytis tulipae. The results of the biological investigations indicate that among the peptides investigated, compounds VII and IX inhibit the growth of plant pathogens P. narcissi and B. tulipae, whereas compounds I and II stimulate the mycelium growth of the aforementioned pathogens. Other peptides show slow antimicrobial activity but do not inhibit the replication of HHV-1 in Vero cells.
    Źródło:
    Pestycydy; 2008, 1-2; 5-11
    0208-8703
    Pojawia się w:
    Pestycydy
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Spektrometria mas w analizie białek i peptydów : znaczniki jonizacyjne
    Mass spectrometry in analysis of peptides and proteins : ionization markers
    Autorzy:
    Bąchor, R.
    Biernat, M.
    Cebrat, M.
    Kijewska, M.
    Kluczyk, A.
    Kuczer, M.
    Paluch, A.
    Waliczek, M.
    Wierzbicka, M.
    Stefanowicz, P.
    Szewczuk, Z.
    Powiązania:
    https://bibliotekanauki.pl/articles/171509.pdf
    Data publikacji:
    2018
    Wydawca:
    Polskie Towarzystwo Chemiczne
    Tematy:
    spektrometria mas
    modyfikacje potranslacyjne
    znaczniki jonizacyjne
    fosforylacja
    glikacja
    biblioteki kombinatoryczne
    mass spectrometry
    post-translational modifications
    ionization markers
    phosphorylation
    glycation
    combinatorial libraries
    Opis:
    High sensitivity, accuracy, and ability to provide structural information makes mass spectrometry (MS) the method of choice for both qualitative and quantitative analysis in proteome research. Peptide sequencing by tandem mass spectrometry (MS/MS) was successfully applied to discover new peptide sequences and modifications. Insufficient ionization of some peptides is one of the main limitations of MS- based peptide identification. The development of sensitive detection techniques for the efficient analysis of such samples is very important. Differences in ionizability cause difficulties in quantification studies, which could be overcome by derivatization of peptides to improve both the detectability and the selectivity of an analysis. Incorporation of ionization markers and isotopic labels (particularly the isobaric tags) is often used for this reason. Isobaric labeling reagents (including commercially available iTRAQ, TMT, DiLeu and DiART) have found a wide application in quantitative proteomics. Mass spectrometry is a very good tool for the determination of posttranslational modifications (PTMs), but the modified proteins are usually present in low concentrations. The development of ionization tags specific to a particular PTM and suitable for sensitive analysis of the modified proteins is required. For the analysis of phosphorylated peptides, a combination of β-elimination and the reaction of resulting α,β-dehydroamino acid residues with the nucleophilic thiol group could be used to detect a labile PTM. Such reaction may be used to introduce derivatizing reagents at the original site of phosphorylation, to enhance ionization in MS analysis. Glycation and glycosylation of proteins are other very important PTMs associated with many natural processes as well as diseases. We have designed and synthesized bifunctional quaternary ammonium salt derivatives of phenylboronic acids for selective detection of carbohydrates and peptide-derived Amadori products by ESI-MS. The attachment of a fixed charge (e.g. in a form of a quaternary ammonium salt) to the amino groups in peptides leads to the enhancement of a precursor ion signal in mass spectra. We have developed several new QAS-containing ionization reagents including bicyclic tags with DABCO, ABCO or azoniaspiro groups. It is worth noting that 2,4,6-substituted pyrylium salts react with amino groups in peptides introducing a stable positive charge and improve peptide detection by MS. The newly developed ionization tags were successfully applied for the analysis of OBOC combinatorial libraries as well as for studying possible biomarkers of preeclampsia, a pregnancy disorder.
    Źródło:
    Wiadomości Chemiczne; 2018, 72, 7-8; 609-633
    0043-5104
    2300-0295
    Pojawia się w:
    Wiadomości Chemiczne
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-2 z 2

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