Interaction of (+)-Strebloside and Its Derivatives with Na+/K+-ATPase and Other Targets
Copyright policy )Interaction of (+)-Strebloside and Its Derivatives with Na+/K+-ATPase and Other Targets
Docking profiles for (+)-strebloside, a cytotoxic cardiac glycoside identified from Streblus asper, and some of its derivatives and Na+/K+-ATPase have been investigated. In addition, binding between (+)-strebloside and its aglycone, strophanthidin, and several of their other molecular targets, including FIH-1, HDAC, KEAP1 and MDM2 (negative regulators of Nrf2 and p53, respectively), NF-κB, and PI3K and Akt1, have been inspected and compared with those for digoxin and its aglycone, digoxigenin. The results showed that (+)-strebloside, digoxin, and their aglycones bind to KEAP1 and MDM2, while (+)-strebloside, strophanthidin, and digoxigenin dock to the active pocket of PI3K, and (+)-strebloside and digoxin interact with FIH-1. Thus, these cardiac glycosides could directly target HIF-1, Nrf2, and p53 protein–protein interactions, Na+/K+-ATPase, and PI3K to mediate their antitumor activity. Overall, (+)-strebloside seems more promising than digoxin for the development of potential anticancer agents.
- The Ohio State University United States
- University of Illinois at Chicago United States
- OHIO STATE UNIVERSITY
- University of Illinois at Chicago United States
- THE OHIO STATE UNIVERSITY United States
Digoxin, Kelch-Like ECH-Associated Protein 1, molecular targets, NF-E2-Related Factor 2, Na<sup>+</sup>/K<sup>+</sup>-ATPase, Organic chemistry, Article, Molecular Docking Simulation, Cardiac Glycosides, Phosphatidylinositol 3-Kinases, QD241-441, Strophanthins, cytotoxicity, Humans, (+)-strebloside, Sodium-Potassium-Exchanging ATPase, docking profiles, Protein Binding
Digoxin, Kelch-Like ECH-Associated Protein 1, molecular targets, NF-E2-Related Factor 2, Na<sup>+</sup>/K<sup>+</sup>-ATPase, Organic chemistry, Article, Molecular Docking Simulation, Cardiac Glycosides, Phosphatidylinositol 3-Kinases, QD241-441, Strophanthins, cytotoxicity, Humans, (+)-strebloside, Sodium-Potassium-Exchanging ATPase, docking profiles, Protein Binding
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