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Abstract
Cytoskeletal structures of Apicomplexan parasites are important for parasite replication, motility, invasion to the host cell and survival. Apicortin, an Apicomplexan specific protein appears to be a crucial factor in maintaining stability of the parasite cytoskeletal assemblies. However, the function of apicortin, in terms of interaction with microtubules still remains elusive. Herein, we have attempted to elucidate the function of Plasmodium falciparum apicortin by monitoring its interaction with two main components of parasite microtubular structure, α-tubulin-I and β-tubulin through in silico and in vitro studies. Further, a p25 domain binding generic drug Tamoxifen (TMX), was used to disrupt PfApicortin-tubulin interactions which led to the inhibition in growth and progression of blood stage life cycle of P. falciparum.
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Details
1 Jawaharlal Nehru University, Special Centre for Molecular Medicine, New Delhi, India (GRID:grid.10706.30) (ISNI:0000 0004 0498 924X)
2 Shiv Nadar University, Department of Life Sciences, School of Natural Sciences, Noida, India (GRID:grid.410868.3) (ISNI:0000 0004 1781 342X)
3 Jamia Millia Islamia, Medicinal Chemistry Laboratory, Department of Biosciences, New Delhi, India (GRID:grid.411818.5) (ISNI:0000 0004 0498 8255)
4 Jawaharlal Nehru University, Special Centre for Molecular Medicine, New Delhi, India (GRID:grid.10706.30) (ISNI:0000 0004 0498 924X); Shiv Nadar University, Department of Life Sciences, School of Natural Sciences, Noida, India (GRID:grid.410868.3) (ISNI:0000 0004 1781 342X)