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Characterization of trifluralin binding with recombinant tubulin from Trypanosoma brucei
Journal article   Peer reviewed

Characterization of trifluralin binding with recombinant tubulin from Trypanosoma brucei

N.L. Giles, A. Armson and S.A. Reid
Parasitology Research, Vol.104(4), pp.893-903
2009
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Abstract

The binding kinetics of five novel trifluralin analogs with recombinant α- and β-tubulin proteins from Trypanosoma brucei rhodesiense was determined. Native tubulin from rats was used to determine the extent of binding of each analog to mammalian tubulin. The results of this study clearly demonstrate two important characteristics of the binding of these trifluralins to tubulin. Firstly, they have specific affinity for trypanosomal tubulin compared with mammalian tubulin irrespective of the chemical composition of the trifluralin analog tested. Secondly, they have a stronger affinity for trypanosomal α-tubulin compared with trypanosomal β-tubulin. In addition, compounds 1007, 1008, 1016, and 1017 have strong binding affinities for α-tubulin, with limited binding affinity for mammalian tubulin, which indicates that these compounds selectively bind to trypanosomal tubulin.

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Collaboration types
Domestic collaboration
Citation topics
1 Clinical & Life Sciences
1.96 Cell Biology
1.96.311 Microtubule Dynamics
Web Of Science research areas
Parasitology
ESI research areas
Microbiology
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