Feasibility of supercritical fluid chromatography/mass spectrometry of polypeptides with up to 40-mers.
Identifieur interne : 002D27 ( Main/Exploration ); précédent : 002D26; suivant : 002D28Feasibility of supercritical fluid chromatography/mass spectrometry of polypeptides with up to 40-mers.
Auteurs : J. Zheng [États-Unis] ; J D Pinkston ; P H Zoutendam ; L T TaylorSource :
- Analytical chemistry [ 0003-2700 ] ; 2006.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , analysis : Peptides.
- chemical : Carbon Dioxide, Pharmaceutical Preparations, Solvents.
- instrumentation : Chromatography, Supercritical Fluid.
- methods : Chromatography, Supercritical Fluid, Drug Industry, Mass Spectrometry.
- Feasibility Studies.
Abstract
Supercritical fluid chromatography (SFC) provides a number of advantages over traditional HPLC such as speed, practical use of longer columns, a normal-phase retention mechanism, and reduced use of organic solvents. Yet, it has been a technique traditionally limited to relatively nonpolar compounds. The nature of SFC mobile and stationary phases did not allow the elution of ionic compounds or of peptides, except, in the latter case, for the most hydrophobic peptides. The characterization of peptides is critically important for drug discovery and development in the pharmaceutical industry, as well as for a variety of other important applications. Here, for the first time to our knowledge, we show that relatively large peptides (at least 40 mers), containing a variety of acidic and basic residues, can be eluted in SFC. We used trifluoroacetic acid as additive in a CO2/methanol mobile phase to suppress deprotonation of peptide carboxylic acid groups and to protonate peptide amino groups. A 2-ethylpyridine bonded silica column, which was specifically developed for SFC, was used for the majority of this work. The relatively simple mobile phase was compatible with mass spectrometric detection.
DOI: 10.1021/ac052025s
PubMed: 16503605
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en">Supercritical fluid chromatography (SFC) provides a number of advantages over traditional HPLC such as speed, practical use of longer columns, a normal-phase retention mechanism, and reduced use of organic solvents. Yet, it has been a technique traditionally limited to relatively nonpolar compounds. The nature of SFC mobile and stationary phases did not allow the elution of ionic compounds or of peptides, except, in the latter case, for the most hydrophobic peptides. The characterization of peptides is critically important for drug discovery and development in the pharmaceutical industry, as well as for a variety of other important applications. Here, for the first time to our knowledge, we show that relatively large peptides (at least 40 mers), containing a variety of acidic and basic residues, can be eluted in SFC. We used trifluoroacetic acid as additive in a CO2/methanol mobile phase to suppress deprotonation of peptide carboxylic acid groups and to protonate peptide amino groups. A 2-ethylpyridine bonded silica column, which was specifically developed for SFC, was used for the majority of this work. The relatively simple mobile phase was compatible with mass spectrometric detection.</div>
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