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STUDY OF COMPLEXES OF ANIMAL METAL-BINDING PROTEIN WITH PLATINUM CYTOSTATICS

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216305%3A26620%2F12%3APU126961" target="_blank" >RIV/00216305:26620/12:PU126961 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    STUDY OF COMPLEXES OF ANIMAL METAL-BINDING PROTEIN WITH PLATINUM CYTOSTATICS

  • Original language description

    The suggestion of interactions between heavy metals and biologic active molecules haven't been exactly estimated yet. However cadmium, lead or mercury are significant environment pollutants and platinum and arsenic are used as oncologic medicament, they have common characteristic. In organism these compounds are not volatile but they are bounded to other molecules. Interactions between heavy metals and proteins are important for range of physiologic processes like transpiration, photosynthesis or detoxification of organisms. In our experiment an electrochemical profile of interactions between 23 metallothionein fragments and cisplatin was studied. At first 23 MT fragments (decapeptides) were selected given by differences in aminoacids ordering. For the experiment amperometric detection implemented to flow injection analysis system (FIA-ED) was used. However a lot of results were estimated, we focused on complex formation between cisplatin and 23 MT fragments analyzed in various conditions. All the 23 MT fragments interacted with cisplatin, in the optional conditions as equimolar ratio, in physiological conditions of phosphate buffer (pH 7.5) in temperature of 37 degrees C. Based on results obtained we determined an interaction constant which defines an ability of each peptide to make an interaction with cisplatin. The highest IC was found by fragments 18 and 22 and the lowest IC by 1, 15, 12 and 19. We found that the major influence of interaction was done not by the change of near neighbouring aminoacids with the conservative cysteines byt these which were about 2 or 3 of positions far away from cysteiene.

  • Czech name

  • Czech description

Classification

  • Type

    D - Article in proceedings

  • CEP classification

  • OECD FORD branch

    40301 - Veterinary science

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2012

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Article name in the collection

    MENDELNET 2012

  • ISBN

    978-80-7375-836-3

  • ISSN

  • e-ISSN

  • Number of pages

    7

  • Pages from-to

    1265-1271

  • Publisher name

    Neuveden

  • Place of publication

    Neuveden

  • Event location

    Mendel Univ, Fac Agron, Brno

  • Event date

    Nov 21, 2012

  • Type of event by nationality

    CST - Celostátní akce

  • UT code for WoS article

    000366461200148