A library of GlcNAc 6- or 1-phosphate analogues was designed, and each compound was evaluated computationally through docking studies for its binding affinity to AGM1/PGM3. The compounds with the highest binding affinity, as ranked through a docking score, were synthesised and screened for their ability to inhibit the production of UDP-GlcNAc. A glycofused oxazoline analogue showed good inhibition, and gave significant results in vitro.
Paiotta, A., D'Orazio, G., Palorini, R., Ricciardiello, F., Zoia, L., Votta, G., et al. (2018). Design, Synthesis, and Preliminary Biological Evaluation of GlcNAc-6P Analogues for the Modulation of Phosphoacetylglucosamine Mutase 1 (AGM1/PGM3). EUROPEAN JOURNAL OF ORGANIC CHEMISTRY, 2018(17), 1946-1952 [10.1002/ejoc.201800183].
Design, Synthesis, and Preliminary Biological Evaluation of GlcNAc-6P Analogues for the Modulation of Phosphoacetylglucosamine Mutase 1 (AGM1/PGM3)
PAIOTTA, ALICE;D'Orazio, G;Palorini, R;Ricciardiello, F;Zoia, L;Votta, G;De Gioia, L;Chiaradonna, F;La Ferla, B
2018
Abstract
A library of GlcNAc 6- or 1-phosphate analogues was designed, and each compound was evaluated computationally through docking studies for its binding affinity to AGM1/PGM3. The compounds with the highest binding affinity, as ranked through a docking score, were synthesised and screened for their ability to inhibit the production of UDP-GlcNAc. A glycofused oxazoline analogue showed good inhibition, and gave significant results in vitro.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
