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Title: General features of the recognition by tubulin of colchicine and related compounds
Authors: Engelborghs, Yves # ×
Issue Date: Jan-1998
Publisher: Springer verlag
Series Title: European biophysics journal with biophysics letters vol:27 issue:5 pages:437-445
Abstract: The kinetic mechanisms of the binding to tubulin of colchicine and eight different analogues have been studied to elucidate details of the recognition mechanism. All of the analogues follow a two step binding mechanism i.e. binding occurs via an initial step with low affinity, followed by an isomerisation of the initial complex leading to the final high affinity state. For several analogues the kinetic and thermodynamic data of both processes are compared here. For all the analogues the Delta G(1)degrees of initial binding at 25 degrees C varies between -13.3 and -28.8 kJ.mol(-1). For the second step Delta G(2)degrees varies between -2.4 and -27 kJ.mol(-1). These limited ranges of free energy change are, however, obtained by a great variety of enthalpy changes and compensatory entropy changes. Comparison of the data for the first and second steps indicates that structural alterations of the drugs always change the thermodynamic parameters of the two steps, and the changes in the first and the second steps are in opposite directions. The fact that this range of experimental behaviour can be incorporated into a general mechanism encourages the extension of these investigations to other colchicine analogues and related compounds with potential pharmaceutical applications.
URI: 
ISSN: 0175-7571
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biochemistry, Molecular and Structural Biology Section
× corresponding author
# (joint) last author

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