Autor: |
Fischer, Thomas, Koulas, Symeon M., Tsagkarakou, Anastasia S., Kyriakis, Efthimios, Stravodimos, George A., Skamnaki, Vassiliki T., Liggri, Panagiota G.V., Zographos, Spyros E., Riedl, Rainer, Leonidas, Demetres D. |
Předmět: |
|
Zdroj: |
Molecules; Apr2019, Vol. 24 Issue 7, p1322-1322, 1p |
Abstrakt: |
Structure-based design and synthesis of two biphenyl-N-acyl-β-d-glucopyranosylamine derivatives as well as their assessment as inhibitors of human liver glycogen phosphorylase (hlGPa, a pharmaceutical target for type 2 diabetes) is presented. X-ray crystallography revealed the importance of structural water molecules and that the inhibitory efficacy correlates with the degree of disturbance caused by the inhibitor binding to a loop crucial for the catalytic mechanism. The in silico-derived models of the binding mode generated during the design process corresponded very well with the crystallographic data. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
|
Nepřihlášeným uživatelům se plný text nezobrazuje |
K zobrazení výsledku je třeba se přihlásit.
|