Applications of Microfluidic Devices with Mass Spectrometry Detection in Proteomics

Abstract

Mass spectrometry (MS) was first used as a detection tool for microfluidic devices in the late nineties (Figeys et al., Anal Chem 69:3153–3160, 1997; Ramsey and Ramsey, Anal Chem 69:1174–1178, 1997; Xue et al., Anal Chem 69:426–430, 1997), and since then, significant efforts have been invested in the further development of efficient microfluidic-MS interfaces and the exploration of microfluidic-MS applicability in biomolecular analysis. Microfluidic devices can be coupled to MS through both electrospray ionization (ESI) and matrix-assisted laser desorption ionization (MALDI) interfaces. Both conventional, such as capillary electrophoresis (CE)/high performance liquid chromatography (HPLC) liquid sheath, liquid junction and micro/nano-ESI interfaces, as well as novel interfaces based on unique features enabled by microfabrication, have been developed. Current protein identification protocols proceed through a series of steps that are generally time-consuming and labor-intensive. The development of microfluidic devices with MS detection has facilitated protein analysis by minimizing sample consumption and enabling high-throughput, automatic sample manipulations. In this chapter, the applicability of microfluidic chips with MS detection in proteomics research is reviewed. Applications that focus on protein analysis, including sample pretreatment, proteolytic digestion and separation are described. Recent progress on cell culture and lysis, protein quantitation, and analysis of protein posttranslational modifications is discussed.