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• W647560311 abstract "1. Multihisztidin peptidek rez(II)- es cink(II)komplexei: A hisztidin nitrogen donoratomok a peptidek elsődleges femkotőhelyei. Ezek koordinaciojaval makrokelatok kepződhetnek, amelyek stabilitasa a hisztidinek szamatol es tavolsagatol fugg. A karboxilcsoportok jelenlete a cink(II)komplexek stabilitasat noveli. A rez(II)ionok az amidcsoport deprotonalodasat is indukalhatjak, ami tobbmagvu komplexek kepződesehez vezet. A megkotott rezionok szama megegyezik a hisztidinek szamaval. 2. A prion protein peptid fragmenseinek femkomplexei: Az oktarepeaten kivuli hisztidinek is stabilis rezkotőhelyek. A HuPrP(84-114) fragmensre kapott eredmenyek szerint a kotesi helyek stabilitasi sora: His111 > His96 >> His85. Egyeb atmenetifemek komplexeit is tanulmanyoztuk, amelyek stabilitasi sora a kovetkező: Pd(II) > Cu(II) > Ni(II) > Zn(II) > Cd(II) ~ Co(II) > Mn(II). 3. Az amyloid-? peptid rez(II)komplexei: Az A?(1-16) peptidnek kiugroan nagy rezionaffinitasa van. A terminalis aminocsoport az elsődleges femkotőhely, amit a hisztidinek koordinacioja kovet. Egy A?(1-16) molekula 4 reziont kepes megkotni. Az egy- ket- es harom-magvu komplexeknek koordinacios izomerjei lehetnek, de a terminalis aminocsoport es a szomszedos amidnitrogenek koordinacioja preferalt. | 1. Copper(II) and zinc(II) complexes of multihistidine peptides: Histidyl residues are the primary metal binding sites resulting in the formation of macrochelates. The stabilities of macrochelates are influenced by the number and location of histidyl residues. The stability of zinc(II) complexes is enhanced by the presence of carboxylate functions. Formation of polynuclear complexes has also been detected and their nuclearities correspond to the number of histidyl sites. 2. Metal binding affinity of prion peptide fragments: Histidyl residues outside the octarerepat domain are effective copper binding sites. The results obtained for the copper(II) complexes of HuPrP(84-114) revealed the following stability order: His111 > His96 >> His85. Complex formation with several other transition elements has also been studied and their stability order: Pd(II) > Cu(II) > Ni(II) > Zn(II) > Cd(II) ~ Co(II) > Mn(II). 3. Copper(II) complexes of amyloid-? peptide fragments: A?(1-16) has an outstanding affinity towards the complexation with copper. The terminal amino group is the primary metal binding site, followed by the coordination of histidyl residues. One molecule of A?(1-16) can bind as much as four copper(II) ions. Various coordination isomers of the mono-, di- and tri-nuclear complexes can exist with a preference for the coordination via the terminal amino and subsequent amide groups." @default.
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• W647560311 date "2009-01-01" @default.
• W647560311 modified "2023-10-16" @default.
• W647560311 title "Az átmenetifémionok peptidekkel alkotott komplexei. A fémion-fehérje kölcsönhatás modellezése. = Transition metal complexes of peptides. Models of the metal ion protein interactions." @default.
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