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An antibacterial from Hypericum acmosepalum inhibits ATP-dependent MurE ligase from Mycobacterium tuberculosis

Osman, Khadijo and Evangelopoulos, Dimitrios and Basavannacharya, Chandrakala and Gupta, Antima and McHugh, T.D. and Bhakta, Sanjib and Gibbons, S. (2011) An antibacterial from Hypericum acmosepalum inhibits ATP-dependent MurE ligase from Mycobacterium tuberculosis. International Journal of Antimicrobial Agents 39 (2), pp. 124-129. ISSN 0924-8579.

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Official URL: http://dx.doi.org/10.1016/j.ijantimicag.2011.09.01...

Abstract

In a project to characterise new antibacterial chemotypes from plants, hyperenone A and hypercalin B were isolated from the hexane and chloroform extracts of the aerial parts of Hypericum acmosepalum. The structures of both compounds were characterised by extensive one- and two-dimensional nuclear magnetic resonance (NMR) spectroscopy and were confirmed by mass spectrometry. Hyperenone A and hypercalin B exhibited antibacterial activity against multidrug-resistant strains of Staphylococcus aureus, with minimum inhibition concentration ranges of 2–128 mg/L and 0.5–128 mg/L, respectively. Hyperenone A also showed growth-inhibitory activity against Mycobacterium tuberculosis H37Rv and Mycobacterium bovis BCG at 75 mg/L and 100 mg/L. Neither hyperenone A nor hypercalin B inhibited the growth of Escherichia coli and both were non-toxic to cultured mammalian macrophage cells. Both compounds were tested for their ability to inhibit the ATP-dependent MurE ligase of M. tuberculosis, a crucial enzyme in the cytoplasmic steps of peptidoglycan biosynthesis. Hyperenone A inhibited MurE selectively, whereas hypercalin B did not have any effect on enzyme activity.

Item Type: Article
Additional Information: *Undergrad, left Bbk in 2008
Keyword(s) / Subject(s): Hypericum acmosepalum, Hyperenone A, Hypercalin B, Staphylococcus aureus, Tuberculosis, Peptidoglycan, MurE ligase
School or Research Centre: Birkbeck Schools and Research Centres > School of Science > Biological Sciences
Depositing User: Administrator
Date Deposited: 14 Nov 2011 08:27
Last Modified: 17 Apr 2013 12:21
URI: http://eprints.bbk.ac.uk/id/eprint/4371

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