Correlation free-solution capillary electrophoresis migration times of small peptides with physicochemical properties

Chen, N.; Wang, L.; Zhang, Y. K.

doi:10.1007/bf02272260

Cited by 24 publications

(9 citation statements)

References 13 publications

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“…1=3 (12) where the volume balance between equivalent sphere and cylinder indicates that a H = c/(2s/3) 1/3 with s = c/a. Apart from C // = 1, additional numerical data of C > for a cylinder are provided in [60] and fitted here to the following expression (Eq.…”

Section: Cze Of Peptides With Non-spherical Hydrodynamic Shapesmentioning

confidence: 99%

Exploring the evaluation of net charge, hydrodynamic size and shape of peptides through experimental electrophoretic mobilities obtained from CZE

2006

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This work explores the validity of simple CZE models to analyze the electrophoretic mobilities of 102 peptides reported in literature. These models are based mainly on fundamental physicochemical theories providing analytical expressions amenable to relatively simple numerical analysis. Thus, the Linderstrøm-Lang capillary electrophoresis model (LLCEM) and its perturbed version (PLLCEM), proposed and applied previously to the CZE of globular proteins, are adapted and used here for peptides. Also the effects of pK-shifts on net charge, hydration and hydrodynamic size and shape of peptides are analyzed and discussed. Emphasis is placed on the fact that these parameters are physically coupled, and thus a variation in the net charge may produce an appreciable change in the hydrodynamic size of peptides. Within the framework of CZE, peptides may be assumed as having a hydrodynamic volume associated with either spherical or spheroidal particles. The effects on peptide net charge and hydrodynamic size, of electrostatic interaction between a pair of charged groups in the chain and electrical permitivitty around the peptide domain are studied. The predictions of the PLLCEM and LLCEM are in good agreement with results reported previously in the literature. Several limitations concerning these models and some needs for further research are also described.

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Section: Cze Of Peptides With Non-spherical Hydrodynamic Shapesmentioning

confidence: 99%

Exploring the evaluation of net charge, hydrodynamic size and shape of peptides through experimental electrophoretic mobilities obtained from CZE

2006

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“…Both CE and IEC can be used to separate peptides [26,27]. The separation mechanisms in CE and IEC are mainly based on the differences in electrophoretic mobility of the solutes and electrostatic interaction of solutes with stationary phase, respectively.…”

Section: Selectivity and Efficiencymentioning

confidence: 99%

Separation of peptides by strong cation-exchange capillary electrochromatography

Zou

Liu

et al. 2000

Journal of Chromatography A

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“…varies between l/3 and 213 depending on the system and M [34,35]. These equations were used in our work, but Eq.…”

Section: Prediction Of Mobilitiesmentioning

confidence: 99%

Simulation and optimization of peptide separation by capillary electrophoresis

Cifuentes

Poppe

1994

Journal of Chromatography A

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Simulation and optimization of peptide separation by capillary electrophoresis.Cifuentes, A.; Poppe, H. General rightsIt is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. AbstractThe different mobility equations that have appeared in the literature for predicting peptide mobility were compared. A modified equation that relates the mobility of individual proteolytic species of a peptide to its composition has been obtained: Jo = 1758 log(1 + 0.297q)lM0.41', where p is the electrophoretic mobility in 10e9 m'ls -V, q is the integral value of the charge of the species and M its molecular mass. Also, a rough estimation of the set of pK, values for a peptide was developed. The usefulness of this equation together with a computer program for predicting separations of compounds by capillary zone electrophoresis is demonstrated, employing real electropherograms of peptides from the literature or from experiments.

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Correlation free-solution capillary electrophoresis migration times of small peptides with physicochemical properties

Cited by 24 publications

References 13 publications

Exploring the evaluation of net charge, hydrodynamic size and shape of peptides through experimental electrophoretic mobilities obtained from CZE

Exploring the evaluation of net charge, hydrodynamic size and shape of peptides through experimental electrophoretic mobilities obtained from CZE

Separation of peptides by strong cation-exchange capillary electrochromatography

Simulation and optimization of peptide separation by capillary electrophoresis

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