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|Publication type:||Article in scientific journal|
|Type of review:||Peer review (publication)|
|Title:||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|
Koulas, Symeon M.
Tsagkarakou, Anastasia S.
Stravodimos, George A.
Skamnaki, Vassiliki T.
Liggri, Panagiota G.V.
Zographos, Spyros E.
Leonidas, Demetres D.
|Publisher / Ed. Institution:||MDPI|
|Subjects:||N-acyl-β-d-glucopyranosylamine; X-ray crystallography; Glycogen metabolism; Glycogen phosphorylase inhibitor; Structure-based design; Type 2 diabetes; Binding Site; Catalytic domain; Synthetic chemistry technique; Drug design; Enzyme inhibitor; Glucosamine; Glycogen phosphorylase; Human; Hydrogen bonding; Molecular model; Protein binding; Quantitative structure-activity relationship|
|Subject (DDC):||540: Chemistry|
|Abstract:||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.|
|Fulltext version:||Published version|
|License (according to publishing contract):||CC BY 4.0: Attribution 4.0 International|
|Departement:||Life Sciences and Facility Management|
|Appears in collections:||Publikationen Life Sciences und Facility Management|
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|2019_Fischer_high-consistency.pdf||5.88 MB||Adobe PDF|
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