Thermodynamics studies of designed ligands binding to Cel7A using partial-filling capillary electrophoresis
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1199166
- author
- Nilsson, Mikael ; Fagerström, Alexandra LU ; Berg, Ulf LU and Isaksson, Roland
- organization
- publishing date
- 2008
- 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 Inc.
- external identifiers
-
- wos:000252826600004
- scopus:38849091300
- pmid:18081204
- ISSN
- 0173-0835
- DOI
- 10.1002/elps.200700370
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Organic chemistry (S/LTH) (011001240)
- id
- 34ecbd65-eebe-46e1-83f0-81c851127993 (old id 1199166)
- date added to LUP
- 2016-04-01 11:41:44
- date last changed
- 2022-01-26 08:50:32
@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}},
keywords = {{propranolol; entropy; enthalpy; CE; Cel7A}},
language = {{eng}},
number = {{2}},
pages = {{358--362}},
publisher = {{John Wiley & Sons Inc.}},
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}},
doi = {{10.1002/elps.200700370}},
volume = {{29}},
year = {{2008}},
}