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Recent developments in nanoparticle-based MALDI mass spectrometric analysis of phosphoproteomes

Authors:

Institution:

1. Department of Applied Chemistry, S. V. National Institute of Technology, Surat, 395007, India
2. Department of Chemistry, National Sun Yat-Sen University, Kaohsiung, 804, Taiwan
3. School of Pharmacy, College of Pharmacy, Kaohsiung Medical University, Kaohsiung, 806, Taiwan
4. Institue of Medical Science and Technology, National Sun Yat-Sen University, Kaohsiung, 804, Taiwan
5. Doctoral Degree Program in Marine Biotechnology, National Sun Yat-Sen University, Kaohsiung, 804, Taiwan
6. Center for Nanoscience and Nanotechnology, National Sun Yat-Sen University, Kaohsiung, 804, Taiwan

Abstract:

Mass spectrometry-based strategies are widely used for mapping of post-translational modifications of phosphoproteins. However, the presence of large amounts of non-phosphopeptides seriously interferes by suppressing the intensities of signals for phosphopeptides in direct MALDI-MS techniques due to the low stoichiometry of protein phosphorylation. Several MALDI-MS approaches are known which use either nanoparticles (NPs) as affinity probes, or NPs as microwave heat absorbers. They assist in the enrichment of trace levels of phosphopeptides from complex protein digests and require minimal sample pretreatment, digestion times, and sample volume. This leads to enhance sensitivity and selectivity in the analysis of the phosphoproteomes. This review (with 89 refs.) summarizes and discusses recent developments in the field, with a particular focus on the potential use of nanomaterials such as metal oxides, metal NPs, NPs-coated target plates, and as core-shell nanocomposites acting as affinity probes and as heat absorbers in MALDI-MS analysis of phosphoproteomes.

Figure
We discuss recent developments in the field with the focus on the potential use of nanomaterials, including metal oxides, metal NPs, NPs-coated target plate, core-shell microsphere nanocomposites as affinity probes and as heat absorbers to enhance the performance of MALDI-MS to phosphoproteome analysis. Schematic representation of microwave tryptic digest of casein proteins and their enrichment using DDTC-Au NPs as affinity probes.

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