Planta Med 2014; 80 - LP8
DOI: 10.1055/s-0034-1395074

Bioactive metabolites from the Egyptian Red Sea fungi with potential anti-HCV protease effect

U Hawas 1, LA El-Kassem 2, E Fadl 3, A Halwany 4, A Atif 3, W Elkhateeb 3
  • 1Marine Chemistry Department, Faculty of Marine Sciences, King Abdulaziz University, P. O. Box 80207, Jeddah 21589, Kingdom of Saudi Arabia
  • 2Department of Pharmacognosy, National Research Centre, Dokki 12622, Cairo, Egypt
  • 3Chemistry of Natural and Microbial Products Department, National Research Centre, Dokki 12622, Cairo, Egypt
  • 4Department of Pharmacognosy, Faculty of Pharmacy, Cairo University, Kasr El-Aini St. 11562, Cairo, Egypt

Endophytic fungi are generally recognized as one of the most interesting sources of bioactive natural products. They are synergistic to their host and at least some of them are thought to play an important role in the host's defence by producing secondary metabolites to prevent the host from being attacked successfully by fungi and pests [1, 2]. In our ongoing search for bioactive compounds from marine derived fungi we have investigated fifty one endophytic fungal strains isolated from thirty samples of sponges, soft corals and algae, collected from different sites of Egyptian Red Sea. The biological properties of the culture broth extract of each fungus were explored for anti-HCV protease as well as antimicrobial and anticancer activities. The hydroalcoholic extracts of Alternaria alternata, Aspergillus terreus, and Penicillium chrysogenum showed the most potent inhibition of HCV NS3/4A protease with IC50 value of 14, 10 and 20 µg/mL, respectively, they also revealed a selective activity against HCV protease compared to trypsin, a human protease. Of the compounds in these extracts, alternariol, alternariol 9-methyl ether, emodin, 1-methyl emodin, alatinone and ω-hydroxyemodin were shown to have clearly HCV protease inhibitory activity with IC50 12.0, 22.5, 40.2, 32.3, 22.5 and 10.6 µg/mL, respectively.

Keywords: Red Sea, endophytic fungi, 18S rDNA, HCV-protease, anticancer

References:

[1] Stierle, A. et al. (1993) Science 260: 214 – 216.

[2] Strobel, G. et al. (1997) Aust J Bot 45: 1037 – 1082.