Exploiting ion-mobility mass spectrometry for unraveling proteome complexity

Area of Science:

• Analytical Chemistry
• Biochemistry
• Proteomics

Background:

• Ion mobility spectrometry-mass spectrometry (IMS-MS) is increasingly utilized in proteomic research.
• Its adoption is driven by improvements in dynamic range, throughput, quantitation precision, and proteome coverage.
• IMS separates ions based on drift time in an electric field within an inert gas.

Purpose of the Study:

• To provide an introduction to Ion Mobility Spectrometry (IMS) operation modes.
• To describe the advantages and limitations of IMS.
• To discuss the principles and emerging applications of trapped Ion Mobility Spectrometry-Mass Spectrometry (TIMS-MS).

Main Methods:

• Review of IMS operation modes.
• Description of trapped IMS-MS (TIMS-MS) principles, including parallel accumulation-serial fragmentation.
• Analysis of emerging applications in clinical and single-cell proteomics.

Main Results:

• IMS-MS offers enhanced dynamic range and throughput for proteomic analysis.
• TIMS-MS principles are detailed, highlighting parallel accumulation-serial fragmentation.
• Emerging applications demonstrate increased sample throughput and sensitivity.

Conclusions:

• IMS-MS is a rapidly growing technique in proteomics, offering significant advantages.
• TIMS-MS shows promise for high-throughput clinical proteomics and sensitive single-cell proteomics.
• The potential for intact protein analysis using TIMS-MS is also discussed.