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The study was planned to screen the marine actinobacterial extract for the protease inhibitor activity and its anti- Pf activity under  in vitro  and  in vivo  conditions. Out of 100 isolates, only 3 isolates exhibited moderate to high protease inhibitor activities on trypsin, chymotrypsin and proteinase K. Based on protease inhibitor activity 3 isolates were chosen for further studies. The potential isolate was characterized by polyphasic approach and identified as  Streptomyces  sp LK3 (JF710608). The lead compound was identified as peptide from  Streptomyces  sp LK3. The double-reciprocal plot displayed inhibition mode is non-competitive and it confirms the irreversible nature of protease inhibitor. The peptide from  Streptomyces  sp LK3 extract showed significant anti plasmodial activity (IC 50 : 25.78 µg/ml). In  in vivo  model, the highest level of parasitemia suppression (≈45%) was observed in 600 mg/kg of the peptide. These analyses revealed no significant changes were observed in the spleen and liver tissue during 8 dpi. The results confirmed up-regulation of TGF-β and down regulation of TNF-α in tissue and serum level in  PbA  infected peptide treated mice compared to  PbA  infection. The results obtained infer that the peptide possesses anti- Pf activity activity. It suggests that the extracts have novel metabolites and could be considered as a potential source for drug development.

Protease Inhibitors from Marine Actinobacteria as a Potential Source for Antimalarial Compound