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

Issued Date

2017-06-01

Resource Type

Article

ISSN

18790003
01418130

DOI

10.1016/j.ijbiomac.2017.02.094

Other identifier(s)

2-s2.0-85014475698

Rights

Mahidol University

Rights Holder(s)

SCOPUS

Bibliographic Citation

International Journal of Biological Macromolecules. Vol.99, (2017), 358-364

Suggested Citation

Khomsan Tiensomjitr, Samran Prabpai, Palangpon Kongsaeree Characterization of the selective alkylation site in hemoglobin A by dihydroartemisinin with tandem mass spectrometry. International Journal of Biological Macromolecules. Vol.99, (2017), 358-364. doi:10.1016/j.ijbiomac.2017.02.094 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/41849

Research Projects

Organizational Units

Authors

Journal Issue

Thesis

Title

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

Author(s)

Khomsan Tiensomjitr
 Samran Prabpai
 Palangpon Kongsaeree

Other Contributor(s)

Mahidol University

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.

Keyword(s)

Biochemistry, Genetics and Molecular Biology

Availability

URI

https://repository.li.mahidol.ac.th/handle/20.500.14594/41849

Collections

Scopus 2016-2017