Abstract
Mass spectrometry imaging (MSI) allows label-free detection of a wide range of biomolecules and simultaneously provides their spatial distributions. In particular, MSI by matrix-assisted laser desorption/ionization mass spectrometry (MALDI) has been widely used in biomolecule analysis. However, quantitation in MALDI-MSI is limited by matrix-deposition heterogeneity, analyte extraction area, and analyte–matrix cocrystallization. In this chapter, a microstructured PDMS stamp is utilized to precisely control the matrix deposition area and the analyte extraction area. We describe here simple steps—including stamp fabrication, matrix application, and data-acquisition guideline—for the quantitative analysis of adsorbed peptides on hydrophobic surfaces.
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References
Jo K, Heien ML, Thompson LB, Zhong M, Nuzzo RG, Sweedler JV (2007) Mass spectrometric imaging of peptide release from neuronal cells within microfluidic devices. Lab Chip 7(11):1454–1460
Kim J, Mrksich M (2010) Profiling the selectivity of DNA ligases in an array format with mass spectrometry. Nucleic Acids Res 38(1):e2–e2
Zhong M, Lee CY, Croushore CA, Sweedler JV (2012) Label-free quantitation of peptide release from neurons in a microfluidic device with mass spectrometry imaging. Lab Chip 12(11):2037–2045
Beloqui A, Calvo J, Serna S, Yan S, Wilson IBH, Martin-Lomas M, Reichardt NC (2013) Analysis of microarrays by MALDI-TOF MS. Angew Chem Int Ed 52(29):7477–7481
Yoon S, Park S, Kim MS, Lee CY (2018) Concomitant desalting and concentration of neuropeptides on a donut-shaped surface pattern for MALDI mass spectrometry. Chem Commun 54(45):5688–5691
McDonnell LA, Heeren RMA (2007) Imaging mass spectrometry. Mass Spectrom Rev 26(4):606–643
Gessel MM, Norris JL, Caprioli RM (2014) MALDI imaging mass spectrometry: spatial molecular analysis to enable a new age of discovery. J Proteome 107:71–82
Ellis SR, Bruinen AL, Heeren RMA (2014) A critical evaluation of the current state-of-the-art in quantitative imaging mass spectrometry. Anal Bioanal Chem 406(5):1275–1289
Garden RW, Sweedler JV (2000) Heterogeneity within MALDI samples as revealed by mass spectrometric imaging. Anal Chem 72(1):30–36
Park S, Yoon S, Min H, Moon SM, Choi YJ, Kim IS, Lee GH, Kim MS, Seo J, Jung W, Lee CY (2020) Compartmentalized arrays of matrix droplets for quantitative mass spectrometry imaging of adsorbed peptides. Anal Chem 92(13):8715–8721
Huang YY, Zhou W, Hsia KJ, Menard E, Park J-U, Rogers JA, Alleyne AG (2005) Stamp collapse in soft lithography. Langmuir 21(17):8058–8068
Sui G, Wang J, Lee C-C, Lu W, Lee SP, Leyton JV, Wu AM, Tseng H-R (2006) Solution-phase surface modification in intact poly(dimethylsiloxane) microfluidic channels. Anal Chem 78(15):5543–5551
Acknowledgments
This work was supported by the Basic Science Research Program through the National Research Foundation (NRF) of Korea (NRF-2019R1A2C1084928).
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Park, S., Lee, C.Y. (2022). Extraction and Upconcentration of Adsorbates from Precisely Defined Area for Quantitative MALDI Mass Spectrometry Imaging. In: Lee, YJ. (eds) Mass Spectrometry Imaging of Small Molecules. Methods in Molecular Biology, vol 2437. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-2030-4_11
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DOI: https://doi.org/10.1007/978-1-0716-2030-4_11
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Publisher Name: Humana, New York, NY
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