To What Extent is FAIMS Beneficial in the Analysis of Proteins?

Helen J Cooper

doi:10.1007/s13361-015-1326-4

Abstract

High field asymmetric waveform ion mobility spectrometry (FAIMS), also known as differential ion mobility spectrometry, is emerging as a tool for biomolecular analysis. In this article, the benefits and limitations of FAIMS for protein analysis are discussed. The principles and mechanisms of FAIMS separation of ions are described, and the differences between FAIMS and conventional ion mobility spectrometry are detailed. Protein analysis is considered from both the top-down (intact proteins) and the bottom-up (proteolytic peptides) perspective. The roles of FAIMS in the analysis of complex mixtures of multiple intact proteins and in the analysis of multiple conformers of a single protein are assessed. Similarly, the application of FAIMS in proteomics and targeted analysis of peptides are considered.Graphical ᅟ

Highlights

I n contrast to mass spectrometry, ion mobility spectrometry (IMS) relies on the behavior of gas-phase ions in a gaseous medium
field asymmetric waveform ion mobility spectrometry (FAIMS) cannot currently be used for the direct calculation of collision-cross section but that role is fulfilled by conventional ion mobility spectrometry
FAIMS is capable of separating protein conformers, which has potential benefits for top-down proteomics and structural biology

Summary

Introduction

I n contrast to mass spectrometry, ion mobility spectrometry (IMS) relies on the behavior of gas-phase ions in a gaseous medium. FAIMS takes advantage of these differences in ion mobility at high and low electric fields for the separation of ions at ambient pressure [2,3,4]. This technique, whereby ions at atmospheric pressure are separated on the basis of differences in their mobilities in high and low electric fields, goes by many sobriquets.

Results

Conclusion