Characterization of the selective alkylation site in hemoglobin A by dihydroartemisinin with tandem mass spectrometry.
作者信息
Tiensomjitr Khomsan, Prabpai Samran, Kongsaeree Palangpon
机构信息
Department of Chemistry and Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University, Bangkok 10400, Thailand.
Department of Chemistry and Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University, Bangkok 10400, Thailand.
出版信息
Int J Biol Macromol. 2017 Jun;99:358-364. doi: 10.1016/j.ijbiomac.2017.02.094. Epub 2017 Mar 1.
The reaction between the antimalarial drug dihydroartemisinin (DHA) and hemoglobin A (HbA) was investigated in vitro. A fluorescein-tagged artemisinin analog reacted with HbA and fluorescent HbA-drug adducts could be visualized on SDS-PAGE to confirm stable covalent reaction adducts and necessity of the endoperoxide moiety and Fe(II). Mass spectrometric analyses revealed that DHA favourably alkylated protein part rather than heme and the modification site was identified to be at Tyr35 of the beta globin chain.
Zotero 插件