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- Title
Structural Basis of Artemisinin Binding Sites in Serum Albumin with the Combined Use of NMR and Docking Calculations.
- Authors
Primikyri, Alexandra; Papamokos, Georgios; Venianakis, Themistoklis; Sakka, Marianna; Kontogianni, Vassiliki G.; Gerothanassis, Ioannis P.
- Abstract
Artemisinin is known to bind to the main plasma protein carrier serum albumin (SA); however, there are no atomic level structural data regarding its binding mode with serum albumin. Herein, we employed a combined strategy of saturation transfer difference (STD), transfer nuclear Overhauser effect spectroscopy (TR-NOESY), STD–total correlation spectroscopy (STD-TOCSY), and Interligand Noes for PHArmacophore Mapping (INPHARMA) NMR methods and molecular docking calculations to investigate the structural basis of the interaction of artemisinin with human and bovine serum albumin (HSA/BSA). A significant number of inter-ligand NOEs between artemisinin and the drugs warfarin and ibuprofen as well as docking calculations were interpreted in terms of competitive binding modes of artemisinin in the warfarin (FA7) and ibuprofen (FA4) binding sites. STD NMR experiments demonstrate that artemisinin is the main analyte for the interaction of the A. annua extract with BSA. The combined strategy of NMR and docking calculations of the present work could be of general interest in the identification of the molecular basis of the interactions of natural products with their receptors even within a complex crude extract.
- Subjects
SERUM albumin; ARTEMISININ; BINDING sites; OVERHAUSER effect (Nuclear physics); MOLECULAR interactions; CARRIER proteins; ANTIMALARIALS; IBUPROFEN
- Publication
Molecules, 2022, Vol 27, Issue 18, p5912
- ISSN
1420-3049
- Publication type
Article
- DOI
10.3390/molecules27185912