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Interaction of artemisinin protects the activity of antioxidant enzyme catalase: a biophysical study
CSIR-Institute of Minerals & Materials Technology, Bhubaneswar, India; Academy of Scientific & Innovative Research (AcSIR), Uttar Pradesh, Ghaziabad, India.
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). CSIR-Institute of Minerals & Materials Technology, Bhubaneswar, India.
CSIR-Institute of Minerals & Materials Technology, Bhubaneswar, India.
Cancer Biology Laboratory, DBT-Institute of Life Sciences, Bhubaneswar, India.
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2021 (English)In: International Journal of Biological Macromolecules, ISSN 0141-8130, E-ISSN 1879-0003, Vol. 172, p. 418-428Article in journal (Refereed) Published
Abstract [en]

The major antioxidant enzyme catalase is downregulated and the enzyme activity is compromised in various disease conditions such as malarial and cancer. Hence, the restoration and protection of catalase is a promising therapeutic strategy in disease management. In the present study, for the first time we have demonstrated the protective role of well-known anti-malarial drug Artemisinin (ART) on the time and temperature-induced degradation of bovine liver catalase (BLC) activity. The findings at different time intervals and at higher temperature showed the protective role of ART on BLC activity. Molecular docking studies suggested specific binding of ART on BLC through heme group interface which was further supported by cyclic voltammetry and dynamic light scattering study. The stabilization of BLC in presence of ART was mediated through forming a BLC-ART complex with reduced and shifted electrochemical peak and increased hydrodynamic diameter. ART substantially prevents the temperature-induced reduction in α-helical content with simultaneous increment in other secondary structures like antiparallel, parallel, β-turn and random coils. Nevertheless, the protective role of ART was accepted from the enhanced thermal stability and increased Tm value of BLC in presence of ART at higher temperatures. Our results uncover the mechanism of interaction between ART with BLC and suggest the protective role of ART towards spatiotemporal alteration of BLC by preventing the structural and molecular change in BLC. Thus, the findings advocate ART as a potential therapeutic drug for diseases associated with reduced catalase activity.

Place, publisher, year, edition, pages
Elsevier, 2021. Vol. 172, p. 418-428
Keywords [en]
Artemisinin, Biophysical study, Bovine liver catalase, Circular dichroism, Enzyme activity, Protein conformation, Thermal melting
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-180539DOI: 10.1016/j.ijbiomac.2021.01.072ISI: 000619184100042Scopus ID: 2-s2.0-85100211752OAI: oai:DiVA.org:umu-180539DiVA, id: diva2:1530270
Available from: 2021-02-22 Created: 2021-02-22 Last updated: 2023-09-05Bibliographically approved

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Kumari, Kanchan

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