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Hydrophilic interaction liquid chromatography (HILIC) in proteomics

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Boersema, Paul J., Mohammed, Shabaz, Heck, Albert J. R.·2008·Analytical and Bioanalytical Chemistry

Abstract

In proteomics, nanoflow multidimensional chromatography is now the gold standard for the separation of complex mixtures of peptides as generated by in-solution digestion of whole-cell lysates. Ideally, the different stationary phases used in multidimensional chromatography should provide orthogonal separation characteristics. For this reason, the combination of strong cation exchange chromatography (SCX) and reversed-phase (RP) chromatography is the most widely used combination for the separation of peptides. Here, we review the potential of hydrophilic interaction liquid chromatography (HILIC) as a separation tool in the multidimensional separation of peptides in proteomics applications. Recent work has revealed that HILIC may provide an excellent alternative to SCX, possessing several advantages in the area of separation power and targeted analysis of protein post-translational modifications. [figure: see text]

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Metadata

Authors
Boersema, P. J., Mohammed, S., & Heck, A. J. R.
Venue
Analytical and Bioanalytical Chemistry
Published
2008-02-09
Volume
391
Issue
1
Pages
151-159
ISSN
  • 1618-2642 (ISSN-L)
  • 1618-2650
OpenAlex
W2139196828
Cited by
275
References
2
FWCI
8.56
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Hydrophilic interaction liquid chromatography (HILIC) in proteomics. https://app.cochat.ai/papers/10.1007/s00216-008-1865-7
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Boersema, P. J., Mohammed, S., & Heck, A. J. R. (2008). Hydrophilic interaction liquid chromatography (HILIC) in proteomics. Analytical and Bioanalytical Chemistry. https://doi.org/10.1007/s00216-008-1865-7

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