Evaluation of carrier ampholyte-based capillary electrophoresis for separation of peptides and peptide mimetics
Jazyk angličtina Země Německo Médium print
Typ dokumentu hodnotící studie, časopisecké články, práce podpořená grantem
PubMed
18850645
DOI
10.1002/elps.200800193
Knihovny.cz E-zdroje
- MeSH
- amfolytové směsi chemie MeSH
- elektroforéza kapilární metody MeSH
- koncentrace vodíkových iontů MeSH
- kyseliny fosfinové chemie MeSH
- peptidy analýza izolace a purifikace MeSH
- Publikační typ
- časopisecké články MeSH
- hodnotící studie MeSH
- práce podpořená grantem MeSH
- Názvy látek
- amfolytové směsi MeSH
- kyseliny fosfinové MeSH
- peptidy MeSH
Carrier ampholyte-based capillary electrophoresis (CABCE) has recently been introduced as an alternative to CE (CZE) in the classical buffers. In this study, isoelectric BGEs were obtained by fractionation of Servalyt pH 4-9 carrier ampholytes to cuts of typical width of 0.2 pH unit. CABCE feasibility was examined on a series of insect oostatic peptides, i.e. proline-rich di- to decapeptides, and phosphinic pseudopeptides--tetrapeptide mimetics synthesized as a mixture of four diastereomers having the -P(O)(OH)-CH(2)- moiety embedded into the peptide backbone. With identical selectivity, the separation efficiency of CABCE proved to be as good as classical CE for the insect oostatic peptides and better for diastereomers of the phosphinic pseudopeptides. In addition, despite the numerous species present in the narrow pH cuts of carrier ampholytes, CABCE seems to be free of system zones that could hamper the analysis. Peak symmetry was good for moderately to low mobile peptides, whereas some peak distortion due to electromigration dispersion, was observed for short peptides of rather high mobility.
Citace poskytuje Crossref.org
Structure-activity study of new inhibitors of human betaine-homocysteine S-methyltransferase