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Characterization of trifluralin binding with recombinant tubulin from Trypanosoma brucei

Giles, N.L., Armson, A. and Reid, S.A. (2009) Characterization of trifluralin binding with recombinant tubulin from Trypanosoma brucei. Parasitology Research, 104 (4). pp. 893-903.

Link to Published Version: http://dx.doi.org/10.1007/s00436-008-1271-2
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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.

Publication Type: Journal Article
Murdoch Affiliation: School of Veterinary and Biomedical Sciences
School of Nursing & Midwifery
Publisher: Springer Verlag
Copyright: © 2008 Springer-Verlag
URI: http://researchrepository.murdoch.edu.au/id/eprint/3413
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