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

Kód výsledku v IS VaVaI

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Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

D - Stať ve sborníku

CEP obor

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OECD FORD obor

40301 - Veterinary science

Projekt

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Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název statě ve sborníku

MENDELNET 2012

ISBN

978-80-7375-836-3

ISSN

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e-ISSN

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Počet stran výsledku

7

Strana od-do

1265-1271

Název nakladatele

Neuveden

Místo vydání

Neuveden

Místo konání akce

Mendel Univ, Fac Agron, Brno

Datum konání akce

21. 11. 2012

Typ akce podle státní příslušnosti

CST - Celostátní akce

Kód UT WoS článku

000366461200148