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.
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.
Metadata
| 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: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
| Research Centres and Institutes: | Structural Molecular Biology, Institute of (ISMB) |
| Depositing User: | Administrator |
| Date Deposited: | 14 Nov 2011 08:27 |
| Last Modified: | 02 Aug 2023 16:56 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/4371 |
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