Autor: Koliński, Andrzej - Katalog OPAC zbiorów

Skocz do pozycji: 1.

Tytuł:: Assessment of the free binding energy of 1,25-dihydroxyvitamin D3 and its analogs with the human VDR receptor model
Autorzy:: Kamel, Karol
Kolinski, Andrzej
Powiązania:: https://bibliotekanauki.pl/articles/1039678.pdf
Data publikacji:: 2012
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: KH 1060
drug design
docking
EB 1089
vitamin D
RO 25-9022
Opis:: 1,25-dihydroxyvitamin D3 has quite significant anticancer properties, but its strong calcemic effect in principle excludes it as a potential anticancer drug. Currently, a lot of effort is being devoted to develop potent anticancer analogs of 1,25-dihydroxyvitamin D3 that would not induce hypercalcemia during therapy. In this work, the free binding energy of the VDR receptor with 1,25-dihydroxyvitamin D3 and its three potent analogs (EB 1089, KH 1060 and RO 25-9022) is calculated and compared with each other. With this approach, we could estimate the relative binding affinity of the most potent analog, RO 25-9022, and also revealed a quite distinct mechanism of its interaction with VDR.
Źródło:: Acta Biochimica Polonica; 2012, 59, 4; 653-660
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

Artykuł

Skocz do pozycji: 2.

Tytuł:: Computational study of binding of epothilone A to β-tubulin
Autorzy:: Kamel, Karol
Kolinski, Andrzej
Powiązania:: https://bibliotekanauki.pl/articles/1039930.pdf
Data publikacji:: 2011
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: epothilones
β-tubulin
flexible docking
drug design
Opis:: Understanding the interactions of epothilones with β-tubulin is crucial for computer aided rational design of macrocyclic drugs based on epothilones and epothilone derivatives. Despite numerous structure-activity relationship investigations we still lack substantial knowledge about the binding mode of epothilones and their derivatives to β-tubulin. In this work, we reevaluated the electron crystallography structure of epothilone A/β-tubulin complex (PDB entry 1TVK) and proposed an alternative binding mode of epothilone A to β-tubulin that explains more experimental facts.
Źródło:: Acta Biochimica Polonica; 2011, 58, 2; 255-260
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

Artykuł

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