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An LC-IMS-MS platform providing increased dynamic range for high-throughput proteomic studies.

Erin Shammel Baker¹, Eric A Livesay, Daniel J Orton

¹Biological Sciences Division and Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington 99352, USA.

Journal of Proteome Research

|December 17, 2009

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This study shows that liquid chromatography-ion mobility spectrometry-mass spectrometry (LC-IMS-MS) offers superior peptide detection in complex proteomics samples compared to LC-Fourier Transform MS. The LC-IMS-MS platform enhances dynamic range and reduces interference for more comprehensive analysis.

Area of Science:

Proteomics
Analytical Chemistry
Biochemistry

Background:

High-throughput proteomics analysis is crucial for understanding biological systems.
Rapid separation techniques are needed to handle complex biological samples efficiently.
Existing methods may face challenges with dynamic range and signal interference in complex matrices.

Purpose of the Study:

To evaluate a high-throughput platform using short liquid chromatography (LC) gradients coupled with ion mobility spectrometry-mass spectrometry (IMS-MS) for rapid proteomics analysis.
To compare the performance of LC-IMS-MS with LC-Fourier Transform (FT) MS for analyzing complex peptide samples with varying concentrations.

Main Methods:

A 15-minute reversed-phase capillary liquid chromatography (RPLC) separation was employed.

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Published on: March 14, 2013

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Large Scale Non-targeted Metabolomic Profiling of Serum by Ultra Performance Liquid Chromatography-Mass Spectrometry (UPLC-MS)

Large Scale Non-targeted Metabolomic Profiling of Serum by Ultra Performance Liquid Chromatography-Mass Spectrometry (UPLC-MS)

Published on: March 14, 2013

Samples were analyzed using both LC coupled to a Linear Ion Trap Fourier Transform (FT) Mass Spectrometer (MS) and LC coupled to Ion Mobility Spectrometry-Time of Flight (IMS-TOF) MS.

A complex sample was prepared by spiking 20 reference peptides at concentrations ranging from 1 ng/mL to 10 microg/mL into a tryptic digest of mouse blood plasma.

Main Results:

LC-FT MS detected 13 out of 20 spiked peptides at concentrations >=100 ng/mL.
LC-IMS-TOF MS identified 19 out of 20 spiked peptides across all concentration levels.
LC-IMS-TOF MS demonstrated a greater dynamic range, attributed to drift time separation and differences in ion accumulation strategies.

Conclusions:

The LC-IMS-TOF MS platform provides enhanced sensitivity and dynamic range for rapid proteomics analysis of complex samples.
Drift time separation in LC-IMS-MS effectively resolves low-concentration peptides from complex matrices, reducing interference.
LC-IMS-MS is a promising approach for high-throughput, sensitive, and comprehensive proteomics studies.