Next Article in Journal
Virtual Screening Approach to Identify High-Affinity Inhibitors of Serum and Glucocorticoid-Regulated Kinase 1 among Bioactive Natural Products: Combined Molecular Docking and Simulation Studies
Previous Article in Journal
Characterization of the Volatiles and Quality of Hybrid Grouper and Their Relationship to Changes of Microbial Community During Storage at 4 °C
Previous Article in Special Issue
Chemical Profiles of Cultivated Agarwood Induced by Different Techniques
Open AccessArticle

Anti-Neuraminidase Bioactives from Manggis Hutan (Garcinia celebica L.) Leaves: Partial Purification and Molecular Characterization

1
Department of Pharmaceutical Analysis and Medicinal Chemistry, Faculty of Pharmacy, Universitas Padjadjaran, Jl Raya 21.5 Bandung-Sumedang 45363, Indonesia
2
Department of Pharmaceutical Technology, School of Pharmaceutical Sciences, Universiti Sains Malaysia, P Pinang 11800, Malaysia
3
Pharmaceutical Design and Simulation Laboratory, School of Pharmaceutical Sciences, Universiti Sains Malaysia, P Pinang 11800, Malaysia
*
Authors to whom correspondence should be addressed.
Molecules 2020, 25(4), 821; https://doi.org/10.3390/molecules25040821
Received: 17 January 2020 / Revised: 10 February 2020 / Accepted: 11 February 2020 / Published: 13 February 2020
The neuraminidase enzyme (NA) from the influenza virus is responsible for the proliferation and infections of the virus progeny, prompting several efforts to discover and optimize effective neuraminidase inhibitors. The main aim of this study is to discover a new potential neuraminidase inhibitor that comes from Garcinia celebica leaves (GCL). The bioassay-guided isolation method was performed to obtain lead compounds. The binding interaction of the isolated compounds was predicted by using molecular docking studies. Friedeline (GC1, logP > 5.0), two lanastone derivatives (methyl-3α,23-dihydroxy-17,14-friedolanstan-8,14,24-trien-26-oat (GC2) and 24E-3a,9,23-trihydroxy-17,14-friedolanostan-14,24-dien-26-oate (GC3) with LogP > 5.0) and catechin (GC4, LogP = 1.4) were identified. The inhibitory potency of these four compounds on NA from C. perfringens and H1N1 was found to be as follows: GC4 > GC2 > GC3 > GC1. All compounds exhibited higher inhibitory activity towards C. perfringens NA compared to H1N1 NA. From the molecular docking results, GC4 favorably docked and interacted with Arg118, Arg371, Arg292, Glu276 and Trp178 residues, whilst GC2 interacted with Arg118, Arg371, Arg292, Ile222, Arg224 and Ser246. GC3 interacted with Tyr406 only. GC4 had potent NA inhibition with free energy of binding of −12 kcal/mol. In the enzyme inhibition study, GC4 showed the highest activity with an IC50 of 60.3 µM and 91.0 µM for C. perfringens NA and H1N1 NA—respectively. View Full-Text
Keywords: Garcinia celebica; catechin; friedeline; lanastone; molecular docking Garcinia celebica; catechin; friedeline; lanastone; molecular docking
Show Figures

Figure 1

MDPI and ACS Style

Muchtaridi, M.; Sugijanto, M.; Mohd Gazzali, A.; Wahab, H.A. Anti-Neuraminidase Bioactives from Manggis Hutan (Garcinia celebica L.) Leaves: Partial Purification and Molecular Characterization. Molecules 2020, 25, 821.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop