Comparison of reversed-phase liquid chromatography and hydrophilic interaction/cation-exchange chromatography for the separation of amphipathic alpha-helical peptides with L- and D-amino acid substitutions in the hydrophilic face
Mixed-mode hydrophilic interaction/cation-exchange chromatography (HILIC/CEX) is a novel high-performance technique which has excellent potential for peptide separations. Separations by HILIX/CEX are carried out by subjecting peptides to linear increasing salt gradients in the presence of high levels of acetonitrile, which promotes hydrophilic interactions overlaid on ionic interactions with the cation-exchange matrix. In the present study, HILIC/CEX has been compared to reversed-phase liquid chromatography (RP-HPLC) for separation of mixtures of diastereomeric amphipathic alpha-helical peptide analogues, where L- and D-amino acid substitutions were made in the centre of the hydrophilic face of the amphipathic alpha-helix. Unlike RP-HPLC, temperature had a substantial effect on HILIC/CEX of the peptides, with a rise in temperature from 25 to 65 degrees C increasing the retention times of the peptides as well as improving resolution. Our results again highlight the potential of HILIC/CEX as a peptide separation mode in its own right as well as an excellent complement to RP-HPLC.
Medienart: |
Artikel |
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Erscheinungsjahr: |
2003 |
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Erschienen: |
2003 |
Enthalten in: |
Zur Gesamtaufnahme - volume:1009 |
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Enthalten in: |
Journal of chromatography. A - 1009(2003), 1-2 vom: 15. Aug., Seite 61-71 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Hartmann, Eva [VerfasserIn] |
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Themen: |
Amino Acids |
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Anmerkungen: |
Date Completed 23.04.2004 Date Revised 20.07.2019 published: Print Citation Status MEDLINE |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM134248570 |
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100 | 1 | |a Hartmann, Eva |e verfasserin |4 aut | |
245 | 1 | 0 | |a Comparison of reversed-phase liquid chromatography and hydrophilic interaction/cation-exchange chromatography for the separation of amphipathic alpha-helical peptides with L- and D-amino acid substitutions in the hydrophilic face |
264 | 1 | |c 2003 | |
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500 | |a Date Completed 23.04.2004 | ||
500 | |a Date Revised 20.07.2019 | ||
500 | |a published: Print | ||
500 | |a Citation Status MEDLINE | ||
520 | |a Mixed-mode hydrophilic interaction/cation-exchange chromatography (HILIC/CEX) is a novel high-performance technique which has excellent potential for peptide separations. Separations by HILIX/CEX are carried out by subjecting peptides to linear increasing salt gradients in the presence of high levels of acetonitrile, which promotes hydrophilic interactions overlaid on ionic interactions with the cation-exchange matrix. In the present study, HILIC/CEX has been compared to reversed-phase liquid chromatography (RP-HPLC) for separation of mixtures of diastereomeric amphipathic alpha-helical peptide analogues, where L- and D-amino acid substitutions were made in the centre of the hydrophilic face of the amphipathic alpha-helix. Unlike RP-HPLC, temperature had a substantial effect on HILIC/CEX of the peptides, with a rise in temperature from 25 to 65 degrees C increasing the retention times of the peptides as well as improving resolution. Our results again highlight the potential of HILIC/CEX as a peptide separation mode in its own right as well as an excellent complement to RP-HPLC | ||
650 | 4 | |a Comparative Study | |
650 | 4 | |a Journal Article | |
650 | 4 | |a Research Support, Non-U.S. Gov't | |
650 | 4 | |a Research Support, U.S. Gov't, P.H.S. | |
650 | 7 | |a Amino Acids |2 NLM | |
650 | 7 | |a Peptides |2 NLM | |
700 | 1 | |a Chen, Yuxin |e verfasserin |4 aut | |
700 | 1 | |a Mant, Colin T |e verfasserin |4 aut | |
700 | 1 | |a Jungbauer, Alois |e verfasserin |4 aut | |
700 | 1 | |a Hodges, Robert S |e verfasserin |4 aut | |
773 | 0 | 8 | |i Enthalten in |t Journal of chromatography. A |d 1993 |g 1009(2003), 1-2 vom: 15. Aug., Seite 61-71 |w (DE-627)NLM074731416 |x 1873-3778 |7 nnns |
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