Antimicrobial and antivirulence saponins of Mimusops laurifolia leaves

Author:

Mostafa Hayam M A12,Taha Mohamed3,El-Gendy Ahmed O4,Khairalla Ahmed S45,abd El fattah Medhat6,Raslan Mai1

Affiliation:

1. Biotechnology and Life Sciences Department, Faculty of Postgraduate Studies for Advanced Sciences (PSAS), Beni-Suef University , Beni-Suef 62511 , Egypt

2. Beni-Suef University Hospitals, Faculty of Medicine, Beni-Suef University , Beni-Suef 62521 , Egypt

3. Materials Science and Nanotechnology Department, Faculty of Postgraduate Studies for Advanced Sciences (PSAS), Beni-Suef University , Beni-Suef 62511 , Egypt

4. Microbiology and Immunology Department, Faculty of Pharmacy, Beni-Suef University , Beni-Suef 62511 , Egypt

5. Department of Biology, McMaster University , Hamilton, Ontario L8S 4K1 , Canada

6. Department of Botany and Microbiology, Faculty of Science, Beni-Suef University , Beni-Suef 62511 , Egypt

Abstract

Abstract Mimusops laurifolia is a native species restricted to the Red Sea mountains and Gulf of Aden. Its leaves contain saponins with wide range of biological activities. The presented research aimed to prepare saponins-rich extract from n-butanol fraction of M. laurifolia leaves and screen it for promising antimicrobial activities. Minimum inhibitory concentration (MIC) of the prepared saponins against Candida albicans, and their potential anti-pathogenic and antivirulence effects were determined. Different concentrations of the saponins-rich extract were investigated for their antimicrobial potential, particularly against C. albicans, using the agar well diffusion method. To assess the potential antivirulence and antipathogenic effects, we carried out molecular docking of the bioactive saponins against four key enzymes in C. albicans, which are involved in virulence and/or pathogenicity. Different concentrations of the investigated mixture showed notable antifungal activity against C. albicans with an MIC value of 6.4 μg ml−1. Docking analysis of the investigated saponins showed their affinity toward the docked enzymes, particularly saponin 1 with secreted aspartic proteinase 3 and saponin 6 with secreted aspartic proteinase 5. Thereafter, the stability of these two protein-ligand interactions was investigated using molecular dynamics (MD) simulation. The molecular interactions between saponins and the enzymes' active sites were analyzed and discussed.

Publisher

Oxford University Press (OUP)

Subject

Applied Microbiology and Biotechnology

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