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

Nilsson, Mikael; Fagerström, Alexandra LU ; Berg, Ulf LU and Isaksson, Roland (2008) In Electrophoresis 29(2). p.358-362
Abstract
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 cellobiolrydrolase 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 degrees C, and Delta G degrees, Delta H degrees and Delta S degrees 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... (More)
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 cellobiolrydrolase 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 degrees C, and Delta G degrees, Delta H degrees and Delta S degrees 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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
propranolol, entropy, enthalpy, CE, Cel7A
in
Electrophoresis
volume
29
issue
2
pages
358 - 362
publisher
John Wiley & Sons
external identifiers
  • wos:000252826600004
  • scopus:38849091300
ISSN
0173-0835
DOI
10.1002/elps.200700370
language
English
LU publication?
yes
id
34ecbd65-eebe-46e1-83f0-81c851127993 (old id 1199166)
date added to LUP
2008-09-11 10:32:31
date last changed
2017-01-01 04:27:08
@article{34ecbd65-eebe-46e1-83f0-81c851127993,
  abstract     = {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 cellobiolrydrolase 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 degrees C, and Delta G degrees, Delta H degrees and Delta S degrees 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.},
  author       = {Nilsson, Mikael and Fagerström, Alexandra and Berg, Ulf and Isaksson, Roland},
  issn         = {0173-0835},
  keyword      = {propranolol,entropy,enthalpy,CE,Cel7A},
  language     = {eng},
  number       = {2},
  pages        = {358--362},
  publisher    = {John Wiley & Sons},
  series       = {Electrophoresis},
  title        = {Thermodynamics studies of designed ligands binding to Cel7A using partial-filling capillary electrophoresis},
  url          = {http://dx.doi.org/10.1002/elps.200700370},
  volume       = {29},
  year         = {2008},
}