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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
dc.creator | Fischer T., Koulas S.M., Tsagkarakou A.S., Kyriakis E., Stravodimos G.A., Skamnaki V.T., Liggri P.G.V., Zographos S.E., Riedl R., Leonidas D.D. | en |
dc.date.accessioned | 2023-01-31T07:38:04Z | |
dc.date.available | 2023-01-31T07:38:04Z | |
dc.date.issued | 2019 | |
dc.identifier | 10.3390/molecules24071322 | |
dc.identifier.issn | 14203049 | |
dc.identifier.uri | http://hdl.handle.net/11615/71596 | |
dc.description.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. © 2019 by the authors. | en |
dc.language.iso | en | en |
dc.source | Molecules | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85063723135&doi=10.3390%2fmolecules24071322&partnerID=40&md5=6c71a8dc5f3ad916d2f410085dab3beb | |
dc.subject | enzyme inhibitor | en |
dc.subject | glucopyranosylamine | en |
dc.subject | glucosamine | en |
dc.subject | glycogen phosphorylase | en |
dc.subject | protein binding | en |
dc.subject | analogs and derivatives | en |
dc.subject | antagonists and inhibitors | en |
dc.subject | binding site | en |
dc.subject | chemistry | en |
dc.subject | drug design | en |
dc.subject | enzyme active site | en |
dc.subject | human | en |
dc.subject | hydrogen bond | en |
dc.subject | molecular model | en |
dc.subject | quantitative structure activity relation | en |
dc.subject | synthesis | en |
dc.subject | X ray crystallography | en |
dc.subject | Binding Sites | en |
dc.subject | Catalytic Domain | en |
dc.subject | Chemistry Techniques, Synthetic | en |
dc.subject | Crystallography, X-Ray | en |
dc.subject | Drug Design | en |
dc.subject | Enzyme Inhibitors | en |
dc.subject | Glucosamine | en |
dc.subject | Glycogen Phosphorylase | en |
dc.subject | Humans | en |
dc.subject | Hydrogen Bonding | en |
dc.subject | Models, Molecular | en |
dc.subject | Protein Binding | en |
dc.subject | Quantitative Structure-Activity Relationship | en |
dc.subject | MDPI AG | en |
dc.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 | en |
dc.type | journalArticle | en |
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