Separation of small molecular peptides with same amino acid composition but different sequences by capillary electrophoresis
β Scribed by Yue Wu; Jun Xie; Fang Wang; Zilin Chen
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 412 KB
- Volume
- 32
- Category
- Article
- ISSN
- 1615-9306
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β¦ Synopsis
Abstract
The development of new analytical techniques for identifying endogenous peptides in a cell, organ, or organism (the peptidome) is an important work in the fields of peptidomics and proteomics. MS is currently employed as a powerful analytical technique in peptidomics. However, it has a limitation in the identification of peptides with the same amino acid composition but different sequences, as these peptides have the same molecular weights, and generate the same MS spectrum of molecular ions, when MS is used as the detection technique. Therefore, the development of peptide separation techniques like CE and LC coupled with MS is desirable. In this paper, a methodology for the separation of peptides with the same amino acid composition, but different sequences, by CE has been developed using two tripeptides, GlyβSerβPhe and GlyβPheβSer, as a model sample. Excellent separation selectivity was achieved using the separation mode of MEKC. Separation behavior under different conditions and mechanism is discussed.
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Influence of the amino acid sequence and nature of the cyclodextrin on the separation of small peptide enantiomers by capillary electrophoresis using randomly substituted and single isomer sulfated and sulfonated cyclodextrins The separation of dipeptide and tripeptide enantiomers using negatively