3'-axial CH2 OH substitution on glucopyranose does not increase glycogen phosphorylase inhibitory potency. QM/MM-PBSA calculations suggest why.

@article{Manta20123axialCO,
  title={3'-axial CH2 OH substitution on glucopyranose does not increase glycogen phosphorylase inhibitory potency. QM/MM-PBSA calculations suggest why.},
  author={Stella Manta and Andromachi Xipnitou and Christos Kiritsis and Anastassia L. Kantsadi and Joseph M. Hayes and Vicky T Skamnaki and Christos Lamprakis and Maria Kontou and Panagiotis Zoumpoulakis and Spyros E Zographos and Demetres D Leonidas and Dimitri Komiotis},
  journal={Chemical biology & drug design},
  year={2012},
  volume={79 5},
  pages={663-73}
}
Glycogen phosphorylase is a molecular target for the design of potential hypoglycemic agents. Structure-based design pinpointed that the 3'-position of glucopyranose equipped with a suitable group has the potential to form interactions with enzyme's cofactor, pyridoxal 5'-phosphate (PLP), thus enhancing the inhibitory potency. Hence, we have investigated the binding of two ligands, 1-(β-d-glucopyranosyl)5-fluorouracil (GlcFU) and its 3'-CH(2) OH glucopyranose derivative. Both ligands were found… CONTINUE READING