The free solution electrophoretic mobility of peptides by a bead modeling methodology

Pei, Hongxia; Allison, Stuart A.

doi:10.1016/j.chroma.2008.09.019

Cited by 25 publications

(49 citation statements)

References 39 publications

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“…In the absence of complex formation, Boundary Element [39,41] and Bead Element [42][43][44] procedures have been used and these methodologies shall be applied to the ionic strength dependence of the mobility of short peptides.…”

Section: Discussionmentioning

confidence: 99%

“…Strictly speaking, however, this conclusion is limited to particles that can be reasonably modeled as prolate or oblate ellipsoids. For irregularly shaped model particles, there are Boundary Element [17,39,41] and Bead Array [42][43][44] procedures available. For this study, we shall assume that the ''effective sphere'' model is an adequate model for the systems of interest in this work.…”

Section: Electrophoretic Mobility Of a Single Guest Ion In The Absencmentioning

confidence: 99%

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The dependence of the electrophoretic mobility of small organic ions on ionic strength and complex formation

et al. 2010

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The ionic strength dependence of the electrophoretic mobility of small organic anions with valencies up to -3 is investigated in this study. Provided the anions are not too aspherical, it is argued that shape and charge distribution have little influence on mobility. To a good approximation, the electrophoretic mobility of a small particle should be equal to that of a model sphere with the same hydrodynamic radius and same net charge. For small ions, the relaxation effect (distortion of the ion atmosphere from equilibrium due to external electric and flow fields) is significant even for monovalent ions. Alternative procedures of accounting for the relaxation effect are examined. In order to account for the ionic strength dependence of a specific set of nonaromatic and aromatic anions in aqueous solution, it is necessary to include complex formation between the anion with species in the BGE. A number of possible complexes are considered. When the BGE is Tris-acetate, the most important of these involves the complex formed between anion and Tris, the principle cation in the BGE. When the BGE is sodium borate, an anion-anion (borate) complex appears to be important, at least when the organic anion is monovalent. An algorithm is developed to analyze the ionic strength dependence of the electrophoretic mobility. This algorithm is applied to two sets of organic anions from two independent research groups.

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Section: Discussionmentioning

confidence: 99%

Section: Electrophoretic Mobility Of a Single Guest Ion In The Absencmentioning

confidence: 99%

The dependence of the electrophoretic mobility of small organic ions on ionic strength and complex formation

et al. 2010

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“…This approach is well suited for small ions and nanoparticles (hardcore charged spheres) but is not yet applicable to polyelectrolytes due to the lack of suitable theoretical model. Numerical simulations can also be used [26][27][28][29][30][31] but these approaches are computationally time consuming and, as a consequence, limited so far to the study of oligomeric chains.…”

Section: Introductionmentioning

confidence: 99%

Generalized polymer effective charge measurement by capillary isotachophoresis

Chamieh¹,

Koval²,

Besson³

et al. 2014

Journal of Chromatography A

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“…This has been extended to other particles including long 30 and finite 31 rods, axi‐symmetric ellipsoids 32–34, and rigid particles of arbitrary shape and charge distribution 35–37. To deal with the problem of flexible structures in which the model particle passes through many conformational states, a bead modeling methodology (BMM) has been developed and applied to peptides 38–42. A peptide composed of n amino acids is modeled as 2 n beads and this shall be called the B model in this study.…”

Section: Introductionmentioning

confidence: 99%

“…The B model is outlined in Section 2. As the model and procedure for calculating mobilities (BMM) have been discussed at length in previous work 38–42, details shall be kept to a minimum. However, recent refinements in the BMM are included in the Appendix.…”

Section: Introductionmentioning

confidence: 99%

Modeling the electrophoresis of oligoglycines

Allison

Pei

Twahir

et al. 2010

J of Separation Science

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The electrophoretic mobility of low molecular mass oligoglycines is examined in this study using a "coarse-grained" bead modeling methodology [Pei, H., Allison, S. A., J. Chromatogr. A 2009, 1216, 1908-1916]. The advantage of focusing on these peptides is that their charge state is well known [Plasson, R., Cottet, H., Anal. Chem. 2006, 78, 5394-5402] and extensive electrophoretic mobility data are also available in different buffers [Survay, M. A., Goodall, D. M., Wren, S. A. C., Rowe, R. C., J. Chromatogr. A 1996, 741, 99-113] and over a broad range of temperatures [Plasson, R., Cottet, H., Anal Chem. 2005, 77, 6047-6054]. Except for assumptions about peptide secondary structure, the B model has no adjustable parameters. It is concluded that the oligoglycines adopt a random configuration at high temperature (50 degrees C and higher), but more compact conformations at lower temperature. It is proposed that triglycine through pentaglycine adopt compact cyclic structures at low temperature (up to about 25 degrees C) in aqueous solution. At 25 degrees C, buffer interactions are also examined and may or may not influence peptide conformation depending on the buffer species. In a borate buffer at high pH, the mobility data are consistent with complex formation between the oligoglycine and borate anion.

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The free solution electrophoretic mobility of peptides by a bead modeling methodology

Cited by 25 publications

References 39 publications

The dependence of the electrophoretic mobility of small organic ions on ionic strength and complex formation

The dependence of the electrophoretic mobility of small organic ions on ionic strength and complex formation

Generalized polymer effective charge measurement by capillary isotachophoresis

Modeling the electrophoresis of oligoglycines

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