CE-ESI-MS for bottom-up proteomics: Advances in separation, interfacing and applications

Area of Science:

• Analytical Chemistry
• Proteomics
• Biochemistry

Background:

• Capillary Electrophoresis-Electrospray-Mass Spectrometry (CE-ESI-MS) has re-emerged as a powerful technique for peptide and protein digest analysis.
• Recent advancements in hyphenation strategies have significantly enhanced its separation power and sensitivity.
• The period from 2009 to the present has seen notable developments, particularly with co-axial sheath liquid interfaces.

Purpose of the Study:

• To review newly developed hyphenation strategies for CE-ESI-MS.
• To discuss applications of CE-ESI-MS in bottom-up proteomics.
• To provide a comprehensive overview of method development aspects for CE-ESI-MS in proteomics.

Main Methods:

• Discussion of newly developed hyphenation strategies for CE-ESI-MS.
• Analysis of applications in bottom-up proteomics using CE-ESI-MS with co-axial sheath liquid.
• Detailed examination of technical aspects including background electrolyte choice, capillary coating, and loading methods.

Main Results:

• CE-ESI-MS offers high separation power and sensitivity for peptide and protein digest analysis.
• Co-axial sheath liquid interfaces have been instrumental in recent advancements.
• Modeling of peptide migration in capillary electrophoresis is feasible due to the simple separation process.

Conclusions:

• CE-ESI-MS is a highly effective technique for bottom-up proteomics.
• Careful consideration of method development parameters (electrolyte, coating, loading) is crucial for optimal results.
• Future developments are expected to further enhance the capabilities of CE-ESI-MS in proteomics.