High Consistency of Structure-Based Design and X-Ray Crystallography: Design, Synthesis, Kinetic Evaluation and Crystallographic Binding Mode Determination of Biphenyl-N-acyl-β-d-Glucopyranosylamines as Glycogen Phosphorylase Inhibitors.

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:	CRYSTAL structure AMINO acids MOLECULAR docking CHEMICAL reactions HYDROGEN bonding
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
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