A semiempirical model for the electrophoretic mobilities of peptides in free-solution capillary electrophoresis

Grossman, Paul D.; Colburn, Joel C.; Lauer, Henk H.

doi:10.1016/0003-2697(89)90195-4

Cited by 211 publications

(116 citation statements)

References 4 publications

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“…Grossman's equation [27] (as also used in Ref. varies between l/3 and 213 depending on the system and M [34,35].…”

Section: Prediction Of Mobilitiesmentioning

confidence: 99%

“…These values, obtained from the literature [27,36,37], are given in Table 1. In addition we considered a modification of Eq.…”

Section: -4mentioning

confidence: 99%

“…1, while considering that as the total charge on the peptide increases, the effect of other additional charges on its mobility should decrease [27]. However, the curvature described by log(1 + q) is entirely arbitrary, and we preferred to have an adjustable (via the parameter B) curvature.…”

Section: -4mentioning

confidence: 99%

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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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“…Grossman's equation [27] (as also used in Ref. varies between l/3 and 213 depending on the system and M [34,35].…”

Section: Prediction Of Mobilitiesmentioning

confidence: 99%

“…These values, obtained from the literature [27,36,37], are given in Table 1. In addition we considered a modification of Eq.…”

Section: -4mentioning

confidence: 99%

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Simulation and optimization of peptide separation by capillary electrophoresis

Cifuentes

Poppe

1994

Journal of Chromatography A

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“…Thus, it would appear that the different approaches in [112] [120] performed micro-titration of the peptides, found experimentally accurate pK values and used those for calculating Z. Under these last conditions, the correct relationship was found to be a linear one, as predicted by Equation (1).…”

Section: Determination Of Absolute Mobility and Of Its Relation To Chmentioning

confidence: 94%

“…However, Grossman et al [112] proposed a semi-empirical model which related m ep of a range of positively charged peptides to their size, charge and hydrophobicity. The effects of size and charge were determined independently and then combined to show the following relationship:…”

Section: Determination Of Absolute Mobility and Of Its Relation To Chmentioning

confidence: 99%

Capillary electrophoretic analysis of proteins and peptides of biomedical and pharmacological interest

Righetti

2001

Biopharm & Drug Disp

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Capillary electrophoresis (CE) is an automated approach to electrokinetic separations that has had a deep impact in all fields of life sciences, including biomedical and biotechnological research and clinical and forensic practice. The present review highlights aspects of peptides and proteins separations, with particular emphasis on macromolecular analytes of biomedical interest. Among the various CE techniques available, a novel methodology is here illustrated consisting in separations in acidic, isoelectric buffers, which have the advantage of protonating the silica wall, thus minimizing interactions of proteinaceous material with the siliceous surface, while allowing delivery of high voltage gradients, due to their low conductivities. The review ends with applications of CE to the analysis of folding/unfolding/refolding/misfolding of proteins, a field which has deep implications in the biomedical arena, since it is connected to a host of disorders, such as prion protein diseases.

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Modeling the free solution electrophoretic mobility of short DNA fragments

Allison

Mazur

1998

Biopolymers

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Boundary element methods are used to model the free solution electrophoretic mobility of short DNA fragments. The Stern surfaces of the DNA fragments are modeled as plated cylinders that reproduce translational and rotational diffusion constants. The solvent‐accessible and ion‐accessible surfaces are taken to be coincident with the Stern surface. The mobilities are computed by solving simultaneously the coupled Navier–Stokes, Poisson, and ion‐transport equations. The equilibrium electrostatics are treated at the level of the full Poisson–Boltzmann equation and ion relaxation is included. For polyions as highly charged as short DNA fragments, ion relaxation is substantial. At .11 M KCl, the simulated mobilities of a 20 base pair DNA fragment are in excellent agreement with experiment. At .04 M Tris acetate, pH = 8.0, the simulated mobilities are about 10–15% higher than experimental values and this discrepancy is attributed to the relatively large size of the Tris counterion. The length dependence of the mobility at .11 M KCl is also investigated. Earlier mobility studies on lysozyme are reexamined in view of the present findings. In addition to electrophoretic mobilities, the effective polyion charge measured in steady state electrophoresis and its relationship to the preferential interaction parameter γgG is briefly considered. © 1998 John Wiley & Sons, Inc. Biopoly 46: 359–373, 1998

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A semiempirical model for the electrophoretic mobilities of peptides in free-solution capillary electrophoresis

Cited by 211 publications

References 4 publications

Simulation and optimization of peptide separation by capillary electrophoresis

Simulation and optimization of peptide separation by capillary electrophoresis

Capillary electrophoretic analysis of proteins and peptides of biomedical and pharmacological interest

Modeling the free solution electrophoretic mobility of short DNA fragments

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