| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1230161 | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy | 2014 | 6 Pages |
•DHA and 9-OH DHA both induce the heme group of BHb.•DHA and 9-OH DHA both can change the polarity of BHb.•DHA and 9-OH DHA both make BHb unfolding.•The interaction between BHb and DHA is stronger than 9-OH DHA.
The UV–vis absorption, steady state/time resolved fluorescence spectroscopy and synchronous fluorescence, circular dichroism (CD) spectroscopy are used to investigate the interaction mechanisms of dihydroartemisinin (DHA) and 9-hydroxy-dihydroartemisinin (9-OH DHA), respectively. The UV–vis studies present that DHA and 9-OH DHA can disturb the structure of bovine hemoglobin (BHb). Steady state/time resolved and synchronous fluorescence spectroscopy reveal that the binding constant of DHA with BHb is bigger than 9-OH DHA. CD spectra indicate DHA and 9-OH DHA can change the conformation of BHb. The comparison results suggest that the binding of BHb with DHA is more stable and stronger than 9-OH DHA.
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