Quinoline-triazole hybrids inhibit falcipain-2 and arrest the development of Plasmodium falciparum at the trophozoite stage.

ABSTRACT: Falcipain-2 (FP2) is a papain family cysteine protease and a key member of the hemoglobin degradation pathway, a process that is required at erythrocytic stages of Plasmodium falciparum to obtain amino acids. In this study, we report a set of 10 quinoline-triazole-based compounds (T1-T10) which exhibit a good binding affinity for FP2, inhibit its catalytic activity at micromolar concentrations and thereby arrest the parasite growth. Compounds T4 and T7 inhibited FP2 with IC₅₀ values of 16.16 μM and 25.64 μM respectively. Both the compounds T4 and T7 arrested the development of P. falciparum at the trophozoite stage with an EC₅₀ value 21.89 μM and 49.88 μM. These compounds also showed morphological and food-vacuole abnormalities like E-64, a known inhibit

SUBMITTER: Singh A 

PROVIDER: S-EPMC9076119 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature