Activation energy associated with the electromigration of oligosaccharides through viscosity modifier and polymeric additive containing background electrolytes

Abstract

The activation energy related to the electromigration of oligosaccharides can be determined from their measured electrophoretic mobilities at different temperatures. The effects of a viscosity modifier (ethylene glycol) and a polymeric additive (linear polyacrylamide) on the electrophoretic mobility of linear sugar oligomers with α1-4 linked glucose units (maltooligosaccharides) were studied in CE using the activation energy concept. The electrophoretic separations of 8-aminopyrene-1,3,6-trisulfonate-labeled maltooligosaccharides were monitored by LIF detection in the temperature range of 20-50°C, using either 0-60% ethylene glycol (viscosity modifier) or 0-3% linear polyacrylamide (polymeric additive) containing BGEs. Activation energy curves were constructed based on the slopes of the Arrhenius plots. With the use of linear polyacrylamide additive, solute size-dependent activation energy variations were found for the maltooligosaccharides with polymerization degrees below and above maltoheptaose (DP 7), probably due to molecular conformation changes and possible matrix interaction effects.

Profiling the N-Glycan Composition of IgG with Lectins and Capillary Nanogel Electrophoresis

“…In agreement with results reported by others, 26,52,53 decreasing the separation temperature increased the migration time of all of the N -glycan peaks (see Table S-2). A plot of the mobility versus temperature (Figure S-3) revealed nominal change in mobility below 23 °C.…”

On-line enrichment of N-glycans by immobilized metal-affinity monolith for capillary electrophoresis analysis

“…The drop at G8 was probably due to the conformation change from random coil to well defined helical structure as was suggested earlier [39]. Nevertheless, this similar selectivity of the monolith for oligomers presenting a size higher than 2 glucose units (GU) and lower than 15 is therefore well suited for the glycoprotein-derived N-glycans since the size of most plasma glycoprotein N-linked sugars usually ranges from 4 to 15 GU [40].…”

Recent advances in microscale separation techniques for glycome analysis

“…On the contrary, the presence of PEO in the BGE revealed lower active energy for larger maltooligosaccharides. Interestingly, the addition of an organic modifier to the PEO containing BGE somehow canceled the effect of PEO [86]. In brief, these inspiring studies showed the possibility of BGE being addictive in controlling the separation performance of glycan.…”