Interaction of (+)-Strebloside and Its Derivatives with Na+/K+-ATPase and Other Targets

Molecules. 2021 Sep 18;26(18):5675. doi: 10.3390/molecules26185675.

Abstract

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.

Keywords: (+)-strebloside; Na+/K+-ATPase; cytotoxicity; docking profiles; molecular targets.

MeSH terms

  • Cardiac Glycosides* / chemistry
  • Cardiac Glycosides* / pharmacology
  • Digoxin / chemistry
  • Digoxin / pharmacology
  • Humans
  • Kelch-Like ECH-Associated Protein 1 / metabolism
  • Molecular Docking Simulation*
  • NF-E2-Related Factor 2 / metabolism
  • Phosphatidylinositol 3-Kinases / metabolism
  • Protein Binding
  • Sodium-Potassium-Exchanging ATPase* / antagonists & inhibitors
  • Sodium-Potassium-Exchanging ATPase* / metabolism
  • Strophanthins / chemistry
  • Strophanthins / pharmacology

Substances

  • Sodium-Potassium-Exchanging ATPase
  • Cardiac Glycosides
  • Digoxin
  • Strophanthins
  • Kelch-Like ECH-Associated Protein 1
  • NF-E2-Related Factor 2
  • Phosphatidylinositol 3-Kinases