Abstract
In this study, a porous mixed-mode n-alkyl methacrylate-based monolith has been
used in the separation of therapeutic peptides. While the sulfonic acid (SCX) moiety
derived from 2-acrylamido-2-methyl-1-propanesulfonic acid supports the generation
of a stable electroosmotic flow (EOF) at both acidic and basic pH values, the butyl
ligands provide the nonpolar sites for chromatographic resolution. The performance of
the monolith was evaluated regarding the influence of pH on chromatographic resolution
of peptides. The suitability of the butylmethacrylate/SCX monolith for the analysis
of therapeutic peptides containing basic centres, for example arginine, at moderately
high pH 9.5 and the stability to repeat injections of a mixture of peptides was demonstrated.
Separations with efficiencies as high as 5.06105 plates/m were obtained and
the migration behaviour of the peptides at both low (2.8) and high (9.5) pH values could
be rationalised based on their charge, molecular mass/shape and relative hydrophobicities.
| Original language | English |
|---|---|
| Pages (from-to) | 3445-3451 |
| Number of pages | 6 |
| Journal | Electrophoresis |
| Volume | 26 |
| Issue number | 18 |
| DOIs | |
| Publication status | Published - 2005 |
Keywords
- capillary electrochromatography
- monolithic stationary phases
- therapeutic peptides