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PD Dr. Fidele Ntie-Kang



PD Dr. Fidele Ntie-Kang


E-Mail: ntiekfidele(at)

Development of a Searchable Database for Natural Products from Africa and Nature-inspired Discovery of Potential Schistomiasis Drugs from African Medicinal Plants

The African continent is very rich in biodiversity and  some of the medicinal plants growing on the continent have been used by  its local populations in traditional preparations (marcerations,  concoctions, infusions, incisions, steam baths, etc.) for the treatment  of several ailments. The knowledge of the ethnobotanical uses of some of  these plants has motivated research groups spread across the continent  to engage in the isolation and characterisation of the natural products  contained within the barks, roots, stems, leaves, etc. of the medicinal  plants with the view of investigating the ethnobotanical uses and/or  developing phytomedicines based on African medicinal plants. It is our  aim within this study to make available (online) the current knowledge  on ethnobotanical uses of the medicinal plants as well as the three  dimensional (3D) structures, physico-chemical properties and  measured activities of the compounds which have been isolated from  medicinal plants in Central Africa, with the view of assisting in the  drug discovery process.

The current proposal also includes epigenetic drug discovery against Schistosoma mansoni,  targeting histone modifying enzymes. This will comprise zinc dependent  histonedeacetylases (HDACs), NAD dependent histone deacetylases Sirtuins  (Sirt2) and class 1 protein arginine/lysine methyltransferases (RMTs  and KMTs). For most of the enzymes, crystal structures from mammalians  are available in the PDB. S. mansoni histone deacetylase 8 (smHDAC8), for example,  is a functional acetyl-L-lysine  deacetylase that plays an important role in parasite infectivity and is  therefore a relevant target for drug discovery. The determination of  the atomic structures of smHDAC8 in complex with generic HDAC inhibitors  revealed that the architecture of the smHDAC8 active site pocket  differed significantly from its human counterparts and provided a  framework for the development of inhibitors selectively interfering with  schistosome epigenetic mechanisms. For the parasite enzymes only  recently, the crystal structure of smHDAC8 has been solved by the  SEtTReND consortium. For the other parasitic enzymes we will generate  homology models to carry out docking experiments, followed by virtual  screening, synthetic modifications of scaffolds and biological assays in vitro. Most promising molecules will be tested in vivo on cultures of S. mansoni and in Schistosoma infected mice in order to identify and validate useful lead compounds  that could further be exploited and developed as candidate molecules  that can progress to clinical trials.

Further information here: researchgate   


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