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  • Chirální rozpoznávaní bilirubinu a biliverdinu na poly(L-lysinu), poly(D-lysinu), and poly(L-argininu) a jejich miscelách tvořených dodekanátem sodným za různých pH bylo studováno pomocí kombinace vibračního a elektronického cirkulárního dichroismu. Systémy byly studovány jako fyziologické modely vazebných míst na sérových albuminech pro tyto pigmenty. Bylo zjištěno, ze konformace biliverdinu je citlivější na změny pH roztoku než konformace bilirubinu. Struktura biliverdinu se stává víc uzavřená v kyselem prostředí v komplexech s micelami polylysinů. Částečně zploštění a chirální samoskladba u bilirubinu byla pozorována za větších koncentrací v komplexech s polypeptidy. Pro oba pigmenty byla pozorována inverze znamének ECD signálů pro komplexy s PLA při pH 8.5. (cs)
  • Chiral recognition of bilirubin and biliverdin by poly(L-lysine), poly(D-lysine), and poly(L-arginine) and its micelles with dodecanoate ions at different pH was studied using a combination of vibrational and electronic circular dichroism. These systems were studied as the physiologically important model of the binding sites of the pigments and serum albumin. It was shown that biliverdin is more sensitive than bilirubin to pH in the complexes with polypeptides. Its conformation becomes more ?closed? at acidic pH in the complexes with micellar systems with polylysine.. Partial flattening and chiral self-association of bilirubin molecules takes place at higher pigment concentration in pigment-polypeptide systems. The inversions of ECD signals for the both pigments were observed in the systems with PLA at pH 8.5.
  • Chiral recognition of bilirubin and biliverdin by poly(L-lysine), poly(D-lysine), and poly(L-arginine) and its micelles with dodecanoate ions at different pH was studied using a combination of vibrational and electronic circular dichroism. These systems were studied as the physiologically important model of the binding sites of the pigments and serum albumin. It was shown that biliverdin is more sensitive than bilirubin to pH in the complexes with polypeptides. Its conformation becomes more ?closed? at acidic pH in the complexes with micellar systems with polylysine.. Partial flattening and chiral self-association of bilirubin molecules takes place at higher pigment concentration in pigment-polypeptide systems. The inversions of ECD signals for the both pigments were observed in the systems with PLA at pH 8.5. (en)
Title
  • Bilirubin and biliverdin: structural studies by electronic and vibrational circular dichroism
  • Bilirubin a biliverdin: strukturní studia pomocí elektronického a vibračního cirkulárního dichroismu (cs)
  • Bilirubin and biliverdin: structural studies by electronic and vibrational circular dichroism (en)
skos:prefLabel
  • Bilirubin and biliverdin: structural studies by electronic and vibrational circular dichroism
  • Bilirubin a biliverdin: strukturní studia pomocí elektronického a vibračního cirkulárního dichroismu (cs)
  • Bilirubin and biliverdin: structural studies by electronic and vibrational circular dichroism (en)
skos:notation
  • RIV/60461373:22340/08:00020222!RIV09-AV0-22340___
http://linked.open...avai/riv/aktivita
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  • P(IAA400550702), P(OC 135), Z(MSM6046137307)
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  • 357975
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  • RIV/60461373:22340/08:00020222
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  • Bilirubin; Biliverdin; Circular dichroism; Polypeptide; Chiral recognition (en)
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  • [E5488F781194]
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  • Praha
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  • 4th International Student Conference
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  • Urbanová, Marie
  • Goncharova, Iryna
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  • Prof. Ing. Jiří G. K. Ševčík, DrSc. - CONSULTANCY
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  • 80-903103-2-X
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  • 22340
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