Abstract
In the present work, the thermodynamic characterisation of toxofilin–G-actin complex was completed with differential scanning calorimetry. The relative change in the under curve area of the un-complexed G-actin in the presence of varying toxofilin concentrations was used as an indirect indicator of the complex formation. The toxofilin could efficiently bind to G-actin with a K D value of 15.7 µM. Besides its binding activity, toxofilin stabilised the attached actin molecules as the T m value of G-actin increased to 64.19 °C after the complex formation. Based on the findings, it is possible to conclude that even non-mammalian actin-binding proteins can efficiently modify the basic structural and dynamic properties of actin monomers.
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Acknowledgements
This study was supported by a grant from the Hungarian Science Foundation (NKFIH) K112794 (to MNy), grants from the Hungarian National Office for Research and Technology [GVOP-3.2.1.-2004-04-0190/3.0 and GVOP-3.2.1.-2004-04-0228/3.0 (to MNy)] and by the Grant of PTE ÁOK-KA-2013/1 (to GH). This work was also supported by ‘Science, Please! Research Team on Innovation’ (SROP-4.2.2/08/1/2008-0011) programme and by the European Union and the State of Hungary, co-financed by the European Social Fund in the framework of TÁMOP-4.2.4.A/2-11/1-2012-0001 ‘National Excellence Program’. The Setaram Micro DSC-II (Caluire, France) calorimeter was supported by grant from the Hungarian Scientific Research Found (NKFIH) CO-272 (DL). The present scientific contribution is dedicated to the 650th anniversary of the foundation of the University of Pécs, Hungary.
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Takács-Kollár, V., Nyitrai, M., Lőrinczy, D. et al. Calorimetric characterisation of the toxofilin–G-actin complex. J Therm Anal Calorim 131, 1307–1311 (2018). https://doi.org/10.1007/s10973-017-6698-1
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DOI: https://doi.org/10.1007/s10973-017-6698-1