Thermodynamical studies of designed ligands binding to Cel7A using partial-filling capillary electrophoresis

A convenient experimental method for thermodynamical studies based on partial‐filling affinity CE is presented. The advantages of this approach are the possibility to determine binding energies from relatively weak interactions as well as the small amounts of samples consumed. In order to explore th...

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Bibliographic Details
Published in:Electrophoresis 2008, Vol.29 (2), p.358-362
Main Authors: Nilsson, Mikael, Fagerström, Alexandra, Berg, Ulf, Isaksson, Roland
Format: Article
Language:English
Subjects:
Cel7A
Cellulase - chemistry
Electrophoresis, Capillary - methods
Enthalpy
Entropy
Enzymes, Immobilized
Hypocrea - enzymology
Ligands
Propranolol
Propranolol - analogs & derivatives
Propranolol - chemistry
Propranolol - isolation & purification
Stereoisomerism
Thermodynamics
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Summary:A convenient experimental method for thermodynamical studies based on partial‐filling affinity CE is presented. The advantages of this approach are the possibility to determine binding energies from relatively weak interactions as well as the small amounts of samples consumed. In order to explore the affinity and selectivity of the cellobiohydrolase Cel7A, a number of propranolol analogues were recently designed. The affinities of a selection of these ligands were determined in the temperature interval 15–40°C, and ΔG°, ΔH° and ΔS° were obtained by means of Van't Hoff plots. Through these experiments, the importance of the entropy contribution in the complexation between the ligands and Cel7A has been demonstrated.
ISSN:0173-0835
1522-2683
DOI:10.1002/elps.200700370