What is it about?
we report antimalarial potential of triazole-amino acid hybrids and their role in the inhibition of cysteine protease PfFP-2 as its mechanistic aspect.
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Why is it important?
Our findings showed that there is a relationship between food vacuole related hemozoin formation inhibition or decreased free heme and antimalarial IC50 activity of compounds which ultimately leads to the cell death. It makes these compounds as efficient core for further structural optimization and SAR studies for antimalarial drug discovery to combat with lethal malaria.
Perspectives
Compounds 15 and 18 hindered hemoglobin degradation via intra- and extracellular cysteine protease falcipain-2 (PfFP-2) inhibitory activity both in in-vitro and in-vivo in P. falciparum. In molecular docking studies, both compounds bind into the active site of PfFP-2 and block its accessibility to the substrate that leads to the inhibition of target protein further supported by in-vitro analysis.
Vigyasa Singh
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This page is a summary of: Inhibition of Hemoglobin Degrading Protease Falcipain-2 as a Mechanism for Anti-Malarial Activity of Triazole-Amino Acid Hybrids, Current Topics in Medicinal Chemistry, March 2020, Bentham Science Publishers,
DOI: 10.2174/1568026620666200130162347.
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