Abstract
The glycopeptide antibiotic teicoplanin is shown to be a highly effective stationary phase chiral selector for the resolution of underivatized amino-acid and imino-acid enantiomers. Fifty four of these compounds (including all chiral protein amino acids) as well as a number of dipeptides were resolved. Hydro-organic mobile phases are used and no buffers or added salts are needed in most cases. Hence the purified analytes are easily isolated in pure form, if needed, by evaporating of the solvent. The effect of pH, organic modifier type and amount are discussed. The enantioselective separation mechanism is examined using both molecular modeling and retention data. The strongest stereoselective interaction is for carboxy-terminated D-amino-acids. In the case of peptides, it is not necessary for these to be a D-, D-, terminal sequence for strong interactions. In some cases, including Ala-Ala, the L-, D- terminal sequence showed greater interaction with the teicoplanin chiral stationary phase.
Recommended Citation
A. Berthod et al., "Facile Liquid Chromatographic Enantioresolution of Native Amino Acids and Peptides using a Teicoplanin Chiral Stationary Phase," Journal of Chromatography A, vol. 731, no. 1 thru 2, pp. 123 - 137, Elsevier, Apr 1996.
The definitive version is available at https://doi.org/10.1016/0021-9673(95)01198-6
Department(s)
Chemistry
Keywords and Phrases
Amino acids; Chiral stationary phases; Enantiomer separation; Enantioselectivity; Imino acids; LC; Peptides; Teicoplanin
International Standard Serial Number (ISSN)
0021-9673
Document Type
Article - Journal
Document Version
Citation
File Type
text
Language(s)
English
Rights
© 2024 Elsevier, All rights reserved.
Publication Date
19 Apr 1996
PubMed ID
8646327
Comments
U.S. Department of Energy, Grant DE FG02 88ER13819