Arteminsims from sweet wormwood are known to be the important class of antimalarial drugs. Artemisinin-containing therapies have increased, but the mechanism of action of the sesquiterpene lactone endoperoxides is controversial. …
But these molecular determinants were undefined. In an another report thapsigiargin , a sesquiterpene lactone inhibits both mammalian and malarial SERCAs. These findings led to hypothesis that artermisins interact with a region of PfATP6 that binds thapsigargin-binding cleft of malarial and mammalian SERCAs, and are the determinant of the arteminisinin.Based on the previous data and literature, the authors identified PfATP6 as a target site. Using bioinformatics the researchers compared the amino acid sequences of mammalian and malarial SERCAs, and found that the leu263 residue is unique along with few more amino acid. After identification, different mutant were constructed to determine the affinity of arteminsins towards these mutated forms to establish its role of each amino acid towards arteminsins sensitivity.To determine the role of leu263 and other amino acids in PfATP6 doain. Different mutant of PfATP6 were express in Xenopus oocyte and functionality test were performed. It was shown that in case of altered Leu263 sensitivity decreased to almost three fold. Whereas alteration of other amino acids along with leu263 lead to 10 fold decrease in sensitivity. Similarly, introduction of Leu263 in non-sensitive sps. like Plasmodium vivax and P. berghei ether increased or decreased sensitivity. ...
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