Silnie wiążące analogi stanów przejściowych fosforylaz nukleozydów purynowych - analiza oddziaływań w centrum aktywnym, projektowanie i właściwości

Lewandowicz, A.

Artykuł - szczegóły

Tytuł artykułu

Silnie wiążące analogi stanów przejściowych fosforylaz nukleozydów purynowych - analiza oddziaływań w centrum aktywnym, projektowanie i właściwości

Autorzy

Lewandowicz A.

Identyfikatory

Warianty tytułu

Tight binding transition state analogues of purine nucleoside phosphorylase - studies on interactions in active site cavity, design and properties

Języki publikacji

Abstrakty

Inhibicja fosforylazy nukleozydów purynowych stanowi potencjalną drogę do leczenia immunosupresyjnego i przeciwnowotworowego, jak również rozważa się ją jako środek przeciwko malarii, tj. choroby o wzrastającej lekooporności na dotychczasowe schematy leczenia. W pracy przedstawiono analizy oddziaływań w centrum aktywnym izoenzymów fosforylazy nukleozydów purynowych z różnych organizmów dla kompleksów z wieloma analogami stanu przejściowego, opartymi na pierścieniu imminorybitolu, tj. immucilliny H. Pozwoliło to określić zależność powinowactwa od poszczególnych modyfikacji strukturalnych. Przeprowadzone badania nad kinetycznymi efektami izotopowymi, doprowadziły do opracowania struktur stanów przejściowych ludzkiego i zarodźcowego izoenzymu fosforylazy nukleozydów purynowych wskazujących, że silnie wiążący inhibitor powinien mieć charakter późnego stanu przejściowego o cechach jonu oksakarbeniowego. Analiza właściwości kinetycznych i termodynamicznych przedstawionych analogów stanu przejściowego wykazała, że związkiem najlepiej naśladującym cechy stanu przejściowego fosforylazy nukleozydów purynowych jest DADMe-Immucillina H, określona w pracy jako „ponadbarierowy analog stanu przejściowego", ze względu na cechy przypominające stronę produktu na współrzędnej reakcji. Badania spektroskopowe IR/Ramana pokazały, że siła wiązania silnie wiążących analogów stanu przejściowego jest również wynikiem oddziaływania analogu z jonem fosforanowym w centrum aktywnym, gdzie silne oddziaływanie elektrostatyczne prowadzi do deformacji geometrii fosforanu. Analiza kinetyki wskazała na dwufazowy proces wiązania analogu stanu przejściowego, związany ze zmianami konformacji wskutek zmiany stanu protonacyjnego, co zobrazowane zostało badaniami nad izoenzymem z M. Tuberculosis, wykazującymi powolne ustalanie się inhibicji. DADMe-Immucillina H i DADMe-Immucillina G, silnie wiążące analogi oparte na modyfikacji DADMe poprawiającej właściwości immucilliny H, charakteryzują się pikomolowymi stałymi dysocjacji względem ludzkiego izoenzymu jak i fosforylazy z M. tuberculosis. Choć DADMe-Immucillina H, zgodnie z przewidywaniami na podstawie analizy parametrów kinetycznych, wiąże się znacznie słabiej z izoenzymem zarodźcowym, analiza struktury jego centrum aktywnego, pozwoliła znaleźć selektywny inhibitor preferujący bardziej zarodźcową niż ludzką fosforylazę nukleozydów purynowych, 5'-metylotio-immucillinę H i jest to jedyny taki analog obecnie znany. Przeprowadzone badania kinetyczne wykazały również postulowaną tutaj, nowoodkrytą dwufunkcyjność izoenzymu fosforylazy nukleozydów purynowych z zarodźca malarii, przejawiającego aktywność względem inozyny, jak i 5'-metylotioinozyny, przez co zapewnione jest zarówno dostarczanie puryn dla pasożyta, jak i wtórny metabolizm 5'-metylotionukleozydów ze szlaku poliamin, a blokowanie fosforylazy może prowadzić do śmierci zarodźca malarii na drodze dwóch mechanizmów. Przeprowadzone badania in vivo na myszach wykazały doskonałą biodostępność DADMe-Immucilliny H po podaniu doustnym, w tym przenikalność przez błonę erytrocytarną, oraz znaczne, blisko 3-krotne wydłużenie czasu inhibicji w stosunku do poprzednio badanej immucilliny H. Dane te sugerują, że DADMe-Immucillina H może stanowić lepszą alternatywę dla immucilliny H będącej obecnie w fazie prób klinicznych z udziałem pacjentów z rozrostami T-komórkowymi.

The inhibition of purine nucleoside phosphorylase is considered as a potential way for immunosupressive and anticancer treatment, as well as potential remedy against malaria, the disease demonstrating increasing drug resistance. Analysis of interactions in active site cavity of purine nucleoside phosphorylase from different organisms with complexes of transition state analogues was performed. It has enabled to establish structure-inhibition potential relationship. Kinetic isotope effects analysis performed for human and Plasmodium falciparum isoenzymes helped to find the structures of transition states for both isoenzymes. This analysis has shown that tight binding transition state analogue should be characterized by late transition state with oxacarbenium ion character. Kinetic and thermodynamic properties of tested transition state analogues pointed out that the DADMe-Immucillin H is the most accurate mimic of transition state. The compound is described as "the over the barrier transition state analogue" due to positioning transition state from the side of product on the reaction pathway. The binding of transition state analogues has significant contribution from strong interactions with dianionic phosphate present in active site cavity, what was proven by unusual phosphate geometry distortion shown by IR/Raman analysis. The data, together with molecular electrostatic potential analysis suggested that enzyme-TS analogue complex involves protonated form of inhibitor. The binding is a two phases process with conformational changes and the inhibition slow onset was demonstrated by kinetic analysis on purine nucleoside phosphorylase from M. tuberculosis. DADMe-Immucillin H and DADMe-Immucillin G, tight binding transition state analogues based on a new DADMe modification improving immucillin H properties have shown picomolar dissociation constants against human, as well as M. tuberculosis purine nucleoside phosphorylase. Although DADMe-Immucillin H, according to catalytic parameters analysis binds less tightly, the active cavity analysis helped to design a selective inhibitor, 5'-methylthio-immucillin H preferring malarial rather than human isoenzyme, and this is the only one known such a compound. Double specificity of malarial isoenzyme against inosine as well as 5'-methylthioinosine was also postulated on the basis of kinetic data analysis. It maintains purine salvage and 5'-methylthionucleosides recycling from polyamine pathway for parasite, as well provides that the parasite death may be induced more effectively by blocking two metabolic pathways. In vivo studies on mice shown excellent DADMe-Immucillin H bioavability after oral administration, permeability through erythrocyte membrane and significant, almost triple elongation of inhibition time in comparison to previously studied immucillin H. The data are suggesting that DADMe-Immucillin H may become a better alternative for immucillin H being presently in the phase of clinical trials on patients with malignant T-derived proliferative diseases.

Słowa kluczowe

nukleozydy purynowe fosforylaza nukleozydów purynowych inhibitory stan przejściowy

purine nucleoside phosphorylase inhibitors transient state

Wydawca

Wydawnictwo Politechniki Łódzkiej

Czasopismo

Zeszyty Naukowe. Rozprawy Naukowe / Politechnika Łódzka

Rocznik

2005

Tom

Z. 340

Strony

3--81

Opis fizyczny

Bibliogr. 113 poz.

Twórcy

autor

Lewandowicz A.

Międzynarodowy Instytut Biologii Molekularnej i Komórkowej w Warszawie

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