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Characterization of the selective alkylation site in hemoglobin A by dihydroartemisinin with tandem mass spectrometry

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dc.contributor.authorKhomsan Tiensomjitren_US
dc.contributor.authorSamran Prabpaien_US
dc.contributor.authorPalangpon Kongsaereeen_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-12-21T06:47:40Z
dc.date.accessioned2019-03-14T08:02:51Z
dc.date.available2018-12-21T06:47:40Z
dc.date.available2019-03-14T08:02:51Z
dc.date.issued2017-06-01en_US
dc.description.abstract© 2017 Elsevier B.V. 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.en_US
dc.identifier.citationInternational Journal of Biological Macromolecules. Vol.99, (2017), 358-364en_US
dc.identifier.doi10.1016/j.ijbiomac.2017.02.094en_US
dc.identifier.issn18790003en_US
dc.identifier.issn01418130en_US
dc.identifier.other2-s2.0-85014475698en_US
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/20.500.14594/41849
dc.rightsMahidol Universityen_US
dc.rights.holderSCOPUSen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85014475698&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleCharacterization of the selective alkylation site in hemoglobin A by dihydroartemisinin with tandem mass spectrometryen_US
dc.typeArticleen_US
dspace.entity.typePublication
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85014475698&origin=inwarden_US

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