dc.creator | Stravodimos G.A., Chetter B.A., Kyriakis E., Kantsadi A.L., Chatzileontiadou D.S.M., Skamnaki V.T., Kato A., Hayes J.M., Leonidas D.D. | en |
dc.date.accessioned | 2023-01-31T10:04:22Z | |
dc.date.available | 2023-01-31T10:04:22Z | |
dc.date.issued | 2017 | |
dc.identifier | 10.2174/0929867324666161118122534 | |
dc.identifier.issn | 09298673 | |
dc.identifier.uri | http://hdl.handle.net/11615/79502 | |
dc.description.abstract | Glycogen phosphorylase (GP) is a validated pharmaceutical target for the development of antihyperglycaemic agents. Phytogenic polyphenols, mainly flavonoids and pentacyclic triterpenes, have been found to be potent inhibitors of GP. These compounds have both pharmaceutical and nutraceutical potential for glycemic control in diabetes type 2. This review focuses mainly on the most successful (potent) of these compounds discovered to date. The protein-ligand interactions that form the structural basis of their potencies are discussed, highlighting the potential for exploitation of their scaffolds in the future design of new GP inhibitors. © 2017 Bentham Science Publishers. | en |
dc.language.iso | en | en |
dc.source | Current Medicinal Chemistry | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85016162210&doi=10.2174%2f0929867324666161118122534&partnerID=40&md5=5ec56509084edd33d38b3e9095549a6a | |
dc.subject | alpha glucosidase inhibitor | en |
dc.subject | antidiabetic agent | en |
dc.subject | antioxidant | en |
dc.subject | flavonoid | en |
dc.subject | glycogen phosphorylase | en |
dc.subject | glycosyltransferase inhibitor | en |
dc.subject | polyphenol derivative | en |
dc.subject | quercetin | en |
dc.subject | terpenoid derivative | en |
dc.subject | triterpene derivative | en |
dc.subject | enzyme inhibitor | en |
dc.subject | glucose blood level | en |
dc.subject | glycogen phosphorylase | en |
dc.subject | polyphenol | en |
dc.subject | triterpene | en |
dc.subject | allosterism | en |
dc.subject | antidiabetic activity | en |
dc.subject | antioxidant activity | en |
dc.subject | binding affinity | en |
dc.subject | drug binding site | en |
dc.subject | drug conformation | en |
dc.subject | drug design | en |
dc.subject | drug effect | en |
dc.subject | drug potency | en |
dc.subject | drug structure | en |
dc.subject | glycemic control | en |
dc.subject | human | en |
dc.subject | ligand binding | en |
dc.subject | non insulin dependent diabetes mellitus | en |
dc.subject | nonhuman | en |
dc.subject | protein interaction | en |
dc.subject | protein ligand interaction | en |
dc.subject | protein structure | en |
dc.subject | Review | en |
dc.subject | tea | en |
dc.subject | X ray crystallography | en |
dc.subject | animal | en |
dc.subject | antagonists and inhibitors | en |
dc.subject | blood | en |
dc.subject | chemistry | en |
dc.subject | Diabetes Mellitus, Type 2 | en |
dc.subject | glucose blood level | en |
dc.subject | metabolism | en |
dc.subject | Animals | en |
dc.subject | Blood Glucose | en |
dc.subject | Diabetes Mellitus, Type 2 | en |
dc.subject | Enzyme Inhibitors | en |
dc.subject | Glycogen Phosphorylase | en |
dc.subject | Humans | en |
dc.subject | Polyphenols | en |
dc.subject | Triterpenes | en |
dc.subject | Bentham Science Publishers B.V. | en |
dc.title | Phytogenic polyphenols as glycogen phosphorylase inhibitors: The potential of triterpenes and flavonoids for glycaemic control in type 2 diabetes | en |
dc.type | other | en |