Journal article
Characterization of trifluralin binding with recombinant tubulin from Trypanosoma brucei
Parasitology Research, Vol.104(4), pp.893-903
2009
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.
Details
- Title
- Characterization of trifluralin binding with recombinant tubulin from Trypanosoma brucei
- Authors/Creators
- N.L. Giles (Author/Creator) - The University of Western AustraliaA. Armson (Author/Creator) - Murdoch UniversityS.A. Reid (Author/Creator) - Murdoch University
- Publication Details
- Parasitology Research, Vol.104(4), pp.893-903
- Publisher
- Springer Verlag
- Identifiers
- 991005544700607891
- Copyright
- © 2008 Springer-Verlag
- Murdoch Affiliation
- School of Veterinary and Biomedical Sciences; School of Nursing and Midwifery
- Language
- English
- Resource Type
- Journal article
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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