dc.creator | Drakou C.E., Gardeli C., Tsialtas I., Alexopoulos S., Mallouchos A., Koulas S.M., Tsagkarakou A.S., Asimakopoulos D., Leonidas D.D., Psarra A.-M.G., Skamnaki V.T. | en |
dc.date.accessioned | 2023-01-31T07:36:59Z | |
dc.date.available | 2023-01-31T07:36:59Z | |
dc.date.issued | 2020 | |
dc.identifier | 10.1021/acs.jafc.0c04205 | |
dc.identifier.issn | 00218561 | |
dc.identifier.uri | http://hdl.handle.net/11615/71210 | |
dc.description.abstract | Anthocyanins (ACNs) are dietary phytochemicals with an acknowledged therapeutic significance. Pomegranate juice (PJ) is a rich source of ACNs with potential applications in nutraceutical development. Glycogen phosphorylase (GP) catalyzes the first step of glycogenolysis and is a molecular target for the development of antihyperglycemics. The inhibitory potential of the ACN fraction of PJ is assessed through a combination of in vitro assays, ex vivo investigation in hepatic cells, and X-ray crystallography studies. The ACN extract potently inhibits muscle and liver isoforms of GP. Affinity crystallography reveals the structural basis of inhibition through the binding of pelargonidin-3-O-glucoside at the GP inhibitor site. The glucopyranose moiety is revealed as a major determinant of potency as it promotes a structural binding mode different from that observed for other flavonoids. This inhibitory effect of the ACN scaffold and its binding mode at the GP inhibitor binding site may have significant implications for future structure-based drug design endeavors. Copyright © 2020 American Chemical Society. | en |
dc.language.iso | en | en |
dc.source | Journal of Agricultural and Food Chemistry | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85091126673&doi=10.1021%2facs.jafc.0c04205&partnerID=40&md5=f8f4e67e759c92c53db87b9f75343d58 | |
dc.subject | Anthocyanins | en |
dc.subject | Binding energy | en |
dc.subject | Fruit juices | en |
dc.subject | Phosphorylation | en |
dc.subject | Plants (botany) | en |
dc.subject | Glycogen phosphorylase | en |
dc.subject | Implications for futures | en |
dc.subject | In-vitro assays | en |
dc.subject | Inhibitory effect | en |
dc.subject | Molecular targets | en |
dc.subject | Pomegranate juices | en |
dc.subject | Structural basis | en |
dc.subject | Structure based drug designs | en |
dc.subject | X ray crystallography | en |
dc.subject | anthocyanin | en |
dc.subject | enzyme inhibitor | en |
dc.subject | glycogen phosphorylase | en |
dc.subject | plant extract | en |
dc.subject | protein binding | en |
dc.subject | animal | en |
dc.subject | binding site | en |
dc.subject | chemistry | en |
dc.subject | fruit and vegetable juice | en |
dc.subject | Hep-G2 cell line | en |
dc.subject | human | en |
dc.subject | kinetics | en |
dc.subject | Leporidae | en |
dc.subject | pomegranate | en |
dc.subject | protein motif | en |
dc.subject | X ray crystallography | en |
dc.subject | Amino Acid Motifs | en |
dc.subject | Animals | en |
dc.subject | Anthocyanins | en |
dc.subject | Binding Sites | en |
dc.subject | Crystallography, X-Ray | en |
dc.subject | Enzyme Inhibitors | en |
dc.subject | Fruit and Vegetable Juices | en |
dc.subject | Glycogen Phosphorylase | en |
dc.subject | Hep G2 Cells | en |
dc.subject | Humans | en |
dc.subject | Kinetics | en |
dc.subject | Plant Extracts | en |
dc.subject | Pomegranate | en |
dc.subject | Protein Binding | en |
dc.subject | Rabbits | en |
dc.subject | American Chemical Society | en |
dc.title | Affinity Crystallography Reveals Binding of Pomegranate Juice Anthocyanins at the Inhibitor Site of Glycogen Phosphorylase: The Contribution of a Sugar Moiety to Potency and Its Implications to the Binding Mode | en |
dc.type | journalArticle | en |