Recent progress in the combination of molecularly imprinted polymer-based affinity extraction and mass spectrometry for targeted proteomic analysis

Mass spectrometry (MS) has been a powerful essential tool for proteomic analysis, due to its structural identification and throughput. However, the MS analysis of complex biological samples is severely hampered by the complexity of the samples, the low abundance and poor ionization efficiency of analytes and the coexistence of abundant interfering species in the sample matrices. An additional step to selectively enrich target proteins or peptides prior to the MS analysis is therefore critically necessary. Molecularly imprinted polymers (MIPs), as chemically synthesized receptors produced through polymerization of functional monomer(s) in the presence of a template compound, exhibit affinity and specificity to the template. Also, they are easy to prepare, stable and cost efficient. In recent a decade, MIPs have been demonstrated as promising sorbents for sample pretreatment in proteomics research. In this review, we survey recent advances in the combination of MIP-based affinity extraction and MS for targeted proteomic analysis. Various imprinting strategies for unmodified and post-translationally modified proteins and peptides are discussed. The binding properties of the prepared MIPs and the performance of the hyphenated approach are highlighted. Finally, we brief the perspectives and future challenges of the molecular imprinting technology for targeted proteomics analysis.