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Enhancing MALDI-MSI Spatial Proteomics Analysis through Matrix Solution Acidification
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DOI：10.1039/D5AN00446B.png)
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Abstract
En 中文
Mass spectrometry imaging (MSI) is a powerful technique for spatial resolved proteomics analysis; offering rapid data acquisition and high lateral resolution. However; its utility is often constrained by limited proteomics coverage. In this study; we introduce a simple yet effective method to enhance the detection efficiency of matrix-assisted laser desorption/ionization (MALDI)-MSI for both intact proteins and high-mass tryptic peptides in tissues. By reformulating conventional matrices with elevated concentration of formic acid (FA); we observed that significant improvements in imaging performance; including enhanced peak detection and superior image quality. The efficacy of this approach was first validated using sinapinic acid (SA); a widely adopted matrix for intact protein imaging. Notably; the matrix acidification approach exhibited complementary benefits in tryptic peptide MSI. When using matrix α-cyano-4-hydroxycinnamic acid (CHCA) with 5% FA; we observe selective enhancement of high-mass peptides (> 1500 m/z) in MSI; along with improved image quality. Collectively; our results demonstrate the potential of this approach to improve the proteomic coverage in MSI-based spatial proteomics analysis.
Keywords:
mass spectrometry imaging
proteomics coverage
matrix-assisted laser desorption/ionization
formic acid
spatial proteomics