Voltage-assisted capillary LC of peptides using monolithic capillary columns prepared by ring-opening metathesis polymerization
Language English Country Germany Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Capillary Electrochromatography instrumentation methods MeSH
- Collagen metabolism MeSH
- Collagenases metabolism MeSH
- Oligopeptides isolation & purification MeSH
- Peptide Fragments isolation & purification MeSH
- Peptides isolation & purification MeSH
- Polymers chemical synthesis chemistry MeSH
- Serum Albumin, Bovine metabolism MeSH
- Cattle MeSH
- Trypsin metabolism MeSH
- Animals MeSH
- Check Tag
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Collagen MeSH
- Collagenases MeSH
- Oligopeptides MeSH
- Peptide Fragments MeSH
- Peptides MeSH
- Polymers MeSH
- Serum Albumin, Bovine MeSH
- Trypsin MeSH
We examined the use of monolithic capillary columns prepared via ring-opening metathesis polymerization (ROMP) for peptide separation in voltage-assisted capillary LC (voltage-assisted CLC). In order to demonstrate their potential for peptide separation, ROMP-derived monoliths with RP properties were prepared. The preparation procedure of monoliths was transferred from ROMP monoliths optimized for CLC. ROMP monoliths were synthesized within the confines of 200 microm id fused-silica capillaries with a length of 37 cm. After optimization of the chromatographic conditions, the separation performance was tested using a well-defined set of artificial peptides as well as two peptidic mixtures resulting from a tryptic digest of BSA as well as a collagenase digest of collagen. ROMP monoliths showed comparable performance to other monolithic separation media in voltage-assisted CLC published so far. Therefore, we conclude that by optimizing the composition of the ROMP monoliths as well as by using the controlled manner of their functionalization, ROMP monoliths bear a great potential in CLC and CEC.
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Recent developments in CE and CEC of peptides
