Capillary electrophoretic methods applied to the investigation of peptide complexes
Result description
This article gives an overview of the applications of capillary electrophoretic methods to investigate the non-covalent interactions of peptides (peptide complexes) with variable middle- and high-molecular-mass receptors (ligands) as well as with small ions and molecules in the period 2007-2014. Different modes of capillary electrophoretic methods, such as mobility shift (vacancy) affinity capillary electrophoresis, multiple injection affinity capillary electrophoresis, partial filling affinity capillary electrophoresis, Hummel-Dryer method, vacancy peak method and (continuous) frontal analysis capillary electrophoresis, are briefly described and their applicability to determination of binding constants of peptide complexes is discussed. In addition, the detailed experimental conditions of individual applications and the values of binding constants of the particular peptide complexes are presented.
Keywords
affinity capillary electrophoresisbinding constantsnon-covalent interactionspeptidesstability constants
The result's identifiers
Result code in IS VaVaI
Result on the web
DOI - Digital Object Identifier
Alternative languages
Result language
angličtina
Original language name
Capillary electrophoretic methods applied to the investigation of peptide complexes
Original language description
This article gives an overview of the applications of capillary electrophoretic methods to investigate the non-covalent interactions of peptides (peptide complexes) with variable middle- and high-molecular-mass receptors (ligands) as well as with small ions and molecules in the period 2007-2014. Different modes of capillary electrophoretic methods, such as mobility shift (vacancy) affinity capillary electrophoresis, multiple injection affinity capillary electrophoresis, partial filling affinity capillary electrophoresis, Hummel-Dryer method, vacancy peak method and (continuous) frontal analysis capillary electrophoresis, are briefly described and their applicability to determination of binding constants of peptide complexes is discussed. In addition, the detailed experimental conditions of individual applications and the values of binding constants of the particular peptide complexes are presented.
Czech name
—
Czech description
—
Classification
Type
Jx - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CB - Analytical chemistry, separation
OECD FORD branch
—
Result continuities
Project
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Separation Science
ISSN
1615-9306
e-ISSN
—
Volume of the periodical
38
Issue of the periodical within the volume
15
Country of publishing house
DE - GERMANY
Number of pages
14
Pages from-to
2708-2721
UT code for WoS article
000358443600019
EID of the result in the Scopus database
2-s2.0-84937735739
Result type
Jx - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP
CB - Analytical chemistry, separation
Year of implementation
2015