Capillary electrophoretic separation of proteins and peptides by ion-pairing with heptanesulfonic acid

Mikšı́k, Ivan; Charvátová, Jana; Eckhardt, Adam; Cserháti, Tibor; Forgács, Eszter; Deyl, Z.

doi:10.1016/j.jchromb.2003.09.041

Cited by 5 publications

(3 citation statements)

References 9 publications

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“…A class of compounds that has been used successfully as such agents is represented by organic sulfonates. Hexanesulfonic acid, under conditions where it is partly deprotonated, has been shown to enhance separation of polylysines of different lengths . Conversely, the separation of sulfonate analytes can be enhanced by addition of aliphatic compounds containing two or more ammonium groups .…”

Section: Introductionmentioning

confidence: 99%

Counterion condensation in short cationic peptides: Limiting mobilities beyond the Onsager–Fuoss theory

et al. 2012

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We investigated the effect of the background electrolyte (BGE) anions on the electrophoretic mobilities of the cationic amino acids arginine and lysine and the polycationic peptides tetraarginine, tetralysine, nonaarginine, and nonalysine. BGEs composed of sodium chloride, sodium propane-1,3-disulfonate, and sodium sulfate were used. For the amino acids, determination of the limiting mobility by extrapolation, using the Onsager-Fuoss (OF) theory expression, yielded consistent estimates. For the peptides, however, the estimates of the limiting mobilities were found to spuriously depend on the BGE salt. This paradox was resolved using molecular modeling. Simulations, on all-atom as well as coarse-grained levels, show that significant counterion condensation, an effect not accounted for in OF theory, occurs for the tetra- and nonapeptides, even for low BGE concentrations. Including this effect in the quantitative estimation of the BGE effect on mobility removed the discrepancy between the estimated limiting mobilities in different salts. The counterion condensation was found to be mainly due to electrostatic interactions, with specific ion effects playing a secondary role. Therefore, the conclusions are likely to be generalizable to other analytes with a similar density of charged groups and OF theory is expected to fail in a predictable way for such analytes.

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Section: Introductionmentioning

confidence: 99%

Counterion condensation in short cationic peptides: Limiting mobilities beyond the Onsager–Fuoss theory

et al. 2012

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“…There are several other ways to affect mobility of protein analytes, e.g., ion-pairing with heptane sulfonic acid has been used to improve CZE separation of CNBr fragments of several types of collagen [89]. In an approach reminiscent of MEKC, liposomes based on 1-palmitoyl-2-oleyolsn-glycero-3-phosphocholine were used as pseudostationary phase for CE of basic proteins [54,90].…”

Section: Improving Separationmentioning

confidence: 99%

Capillary electrophoresis of proteins 2003–2005

Dolnı́k¹

2006

Electrophoresis

139

117

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This review article with 304 references describes recent developments in CE of proteins, and covers the two years since the previous review (Hutterer, K., Dolník, V., Electrophoresis 2003, 24, 3998-4012) through Spring 2005. It covers topics related to CE of proteins, including modeling of the electrophoretic migration of proteins, sample pretreatment, wall coatings, improving separation, various forms of detection, special electrophoretic techniques such as affinity CE, CIEF, and applications of CE to the analysis of proteins in real-world samples including human body fluids, food and agricultural samples, protein pharmaceuticals, and recombinant protein preparations.

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“…A closely related issue concerns the dependence of peptide mobility on the composition of the BGE and how the composition of the BGE can enhance separations in free solution CE . Recently, Wernersson et al carried out a careful and systematic study of the mobility of lysine, K, arginine, R, and oligos of lysine, and arginine (K 4 , K 9 , R 4 , and R 9 ) in a variety several different BGEs at room temperature and neutral pH.…”

Section: Introductionmentioning

confidence: 99%

Specific ion effects on the electrophoretic mobility of small, highly charged peptides: A modeling study

Allison

Bui

et al. 2014

J of Separation Science

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In this work, we use coarse-grained modeling to study the free solution electrophoretic mobility of small highly charged peptides (lysine, arginine, and short oligos thereof (up to nonapeptides)) in NaCl and Na2SO4 aqueous solutions at neutral pH and room temperature. The experimental data are taken from the literature. A bead modeling methodology that treats the electrostatics at the level of the nonlinear Poisson Boltzmann equation developed previously in our laboratory is able to account for the mobility of all peptides in NaCl, but not Na2SO4. The peptide mobilities in Na2SO4 can be accounted for by including sulfate binding in the model and this is proposed as one possible explanation for the discrepancy. Oligo arginine peptides bind more sulfate than oligo lysines and sulfate binding increases with the oligo length.

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Capillary electrophoretic separation of proteins and peptides by ion-pairing with heptanesulfonic acid

Cited by 5 publications

References 9 publications

Counterion condensation in short cationic peptides: Limiting mobilities beyond the Onsager–Fuoss theory

Counterion condensation in short cationic peptides: Limiting mobilities beyond the Onsager–Fuoss theory

Capillary electrophoresis of proteins 2003–2005

Specific ion effects on the electrophoretic mobility of small, highly charged peptides: A modeling study

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