Journal
JOURNAL OF MEDICINAL CHEMISTRY
Volume 60, Issue 22, Pages 9251-9262Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jmedchem.7b01056
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Funding
- Hungarian Scientific Research Fund [OTKA PD105808]
- EU [GINOP-2.3.2-15-2016-00008]
- European Regional Development Fund
- Department of Biochemistry and Biotechnology, University of Thessaly
- EU under BioStruct-X [283570]
- Hellenic State Scholarships Foundation - Operational Programme Education and Lifelong Learning
- European Social Fund (ESF)
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Aryl substituted 1-(beta-D-glucosaminyl)-1,2,3-triazoles as well as C-beta-D-glucosaminyl 1,2,4-triazoles and imidazoles were synthesized and tested as inhibitors against muscle and liver isoforms of glycogen phosphorylase (GP). While the N-beta-D-glucosaminyl 1,2,3-triazoles showed weak or no inhibition, the C-beta-D-glucosaminyl derivatives had potent activity, and the best inhibitor was the 2-(beta-5-D-glucosaminy1)-4(5)-(2-naphthyl)-imidazole with a K-i value of 143 nM against human liver GPa. An X-ray crystallography study of the rabbit muscle GPb inhibitor complexes revealed structural features of the strong binding and offered an explanation for the differences in inhibitory potency between glucosyl and glucosaminyl derivatives and also for the differences between imidazole and 1,2,4-triazole analogues.
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