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Effective Electrophoretic Mobility (effective + electrophoretic_mobility)

Distribution by Scientific Domains

Chemistry	50%

Selected Abstracts

Cover Picture: Electrophoresis 13'09

ELECTROPHORESIS, Issue 13 2009
Article first published online: 20 JUL 200
Issue 13 is a special issue on "CE and CEC of Amino Acids, Peptides and Proteins" assembling 19 papers on various topics including fast, high efficient and high sensitive "CE and CEC techniques for quality control and purity determination of native and (bio)synthetic amino acids, peptides and proteins, for monitoring of their synthesis, isolation, chemical derivatization and enzymatic digestion and also for investigation of their interactions with other molecules. New methodologies, such as electrodialysis for sample preparation, chiral ligand-exchange CE, immunoaffinity CE, affinity capillary isoelectric focusing, combination of transient isotachophoretic preconcentration with capillary zone electophoresis (CZE) analysis, two-dimensional CE-mass spectrometry (MS) separations and advances in high-sensitive CE-laser induced fluorescence (LIF) and CE-electrochemiluminescence detection schemes, are widely presented here. The applications of CE and CEC methods include chiral analysis of amino acids, determination of low abundant amino acids, peptides and proteins in complex matrices, such as human and animal body fluids and tissue biopsies, and profiling of cell lysates and recombinant proteins, e.g. birch pollen allergen and human interleukin 7. As can be seen from several contributions, preparation of new capillary coatings suppressing the adsorption of peptides and proteins to the fused silica capillary wall in their CZE analyses and/or increasing the selectivity of their open-tubular CEC separations remains a hot topic in the area of CE and CEC developments. In addition, it is shown that through the theoretical modelling of the CZE determined effective electrophoretic mobilities of proteins, the important parameters, such as charge, hydration and shape of their molecules, can be estimated." [source]

Capillary electrophoretic and computational study of the complexation of valinomycin with rubidium cation

ELECTROPHORESIS, Issue 5 2009
Sille Ehala
Abstract This study is focused on the characterization of interactions of valinomycin (Val), a macrocyclic dodecadepsipeptide antibiotic ionophore, with rubidium cation, Rb+. Capillary affinity electrophoresis was employed for the experimental evaluation of the strength of the Val,Rb+ complex. The study involved the measurement of the change of effective electrophoretic mobility of Val at increasing concentration of Rb+ cation in the BGE. From the dependence of Val effective electrophoretic mobility on the Rb+ cation concentration in the BGE (methanolic solution of 100,mM Tris, 50,mM acetic acid, 0,1,mM RbCl), the apparent binding (stability) constant (Kb) of the Val,Rb+ complex in methanol was evaluated as log,Kb=4.63±0.27. According to the quantum mechanical density functional theory calculations employed to predict the most probable structure of Val,Rb+ complex, Val is stabilized by strong non-covalent bond interactions of Rb+ with six ester carbonyl oxygen atoms so that the position of the "central" Rb+ cation in the Val cage is symmetric. [source]

Estimation of global structural and transport properties of peptides through the modeling of their CZE mobility data

JOURNAL OF SEPARATION SCIENCE, JSS, Issue 16 2010
Maria V. Piaggio
Abstract Peptide electrophoretic mobility data are interpreted through a physicochemical CZE model, providing estimates of the equivalent hydrodynamic radius, hydration, effective and total charge numbers, actual ionizing pK, pH-near molecule and electrical permittivity of peptide domain, among other basic properties. In this study, they are used to estimate some peptide global structural properties proposed, providing thus a distinction among different peptides. Therefore, the solvent drag on the peptide is obtained through a characteristic friction power coefficient of the number of amino acid residues, defined from the global chain conformation in solution. As modeling of the effective electrophoretic mobility of peptides is carried out in terms of particle hydrodynamic size and shape coupled to hydration and effective charge, a packing dimension related to chain conformation within the peptide domain may be defined. In addition, the effective and total charge number fractions of peptides provide some clues on the interpretation of chain conformations within the framework of scaling laws. Furthermore, the model estimates transport properties, such as sedimentation, friction and diffusion coefficients. As the relative numbers of ionizing, polar and non-polar amino acid residues vary in peptides, their global structural properties defined here change appreciably. Needs for further research are also discussed. [source]

Theoretical and experimental study of the complexation of valinomycin with ammonium cation

BIOPOLYMERS, Issue 12 2008
í Dybal
Abstract The interactions of valinomycin, macrocyclic depsipeptide antibiotic ionophore, with ammonium cation NH4+ have been investigated. Using quantum mechanical density functional theory (DFT) calculations, the most probable structure of the valinomycin-NH4+ complex species was predicted. In this complex, the ammonium cation is bound partly by three strong hydrogen bonds to three ester carbonyl oxygen atoms of valinomycin and partly by somewhat weaker hydrogen bonds to the remaining three ester carbonyl groups of the valinomycin ligand. The strength of the valinomycin-NH4+ complex was evaluated experimentally by capillary affinity electrophoresis. From the dependence of valinomycin effective electrophoretic mobility on the ammonium ion concentration in the background electrolyte, the apparent binding (association, stability) constant (Kb) of the valinomycin-NH4+ complex in methanol was evaluated as log Kb = 1.52 ± 0.22. © 2008 Wiley Periodicals, Inc. Biopolymers 89: 1055,1060, 2008. This article was originally published online as an accepted preprint. The "Published Online" date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com [source]