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Lepidine B & E as New Target Inhibitors from Lepidium Sativum Seeds Against Four Enzymes of the Pathogen Candida albicans: In Vitro and In Silico Studies

[ Vol. 20 , Issue. 1 ]

Author(s):

Safia Gacemi*, Khedidja Benarous, Santiago Imperial and Mohamed Yousfi   Pages 127 - 138 ( 12 )

Abstract:


Background and Objective: The present paper aims to study the inhibition of Candida albicans growth as candidiasis treatment, using seeds of Lepidium sativum as source.

Methods: In vitro assays were carried out on the antifungal activity of three kinds of extracts from L. sativum seeds against four strains of C. albicans, then testing the same phytochemicals on the inhibition of Lipase (LCR). A new in silico study was achieved using molecular docking, with Autodock vina program, to find binding affinity of two important and major lepidine alkaloids (lepidine E and B) towards the four enzymes secreted by C. albicans as target drugs, responsible of vitality and virulence of this yeast cells: Lipase, Serine/threonine phosphatase, Phosphomannose isomerase and Sterol 14-alpha demethylase (CYP51).

Results: The results of the microdillution assay show that the hexanic and alkaloidal extracts have an antifungal activity with MICs: 2.25 mg/ml and 4.5mg/ml, respectively. However, Candida rugosa lipase assay gives a remarkable IC50 values for the hexanic extract (1.42± 0.04 mg/ml) followed by 1.7± 0.1 and 2.29 ± 0.09 mg/ml of ethyl acetate and alkaloidal extracts respectively. The molecular docking confirms a significant correlation between C. albicans growth and inhibition of crucial enzymes involved in the invasion mechanism and cellular metabolisms, for the first time there were an interesting and new positive results on binding modes of lepidine E and B on the four studied enzymes.

Conclusion: Through this work, we propose Lepidine B & E as potent antifungal drugs.

Keywords:

Lepidium sativum seed, Lipase, anti-fungal, lepidine alkaloids, molecular docking, Candida albicans.

Affiliation:

Department of Biology, Faculty of Sciences, University of Laghouat BP37G 03000, Laghouat, Department of Biology, Faculty of Sciences, University of Laghouat BP37G 03000, Laghouat, Department of biochemistry, Molecular Biomedicine, Faculty of Biology. University of Barcelona, Avenue de Diagonal, 643 08028 Barcelona, Department of Biology, Faculty of Sciences, University of Laghouat BP37G 03000, Laghouat

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