(E)-Propyl α-Cyano-4-Hydroxyl Cinnamylate: A High Sensitive and Salt Tolerant Matrix for Intact Protein Profiling by MALDI Mass Spectrometry

Wang, Sheng; Xiao, Chunsheng; Wang, Huixin; Wang, Bing; Liu, Ying; Chen, Xuesi; Guo, Xinhua

doi:10.1007/s13361-015-1325-5

Cited by 21 publications

(13 citation statements)

References 52 publications

(51 reference statements)

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“…Quite a few publications have proposed new MALDI matrixes over the past 2 years. Wang et al introduced (E)-propyl alpha-cyano-4-hydroxyl cinnamylate (CHCA-C3) as a highly effective matrix for protein ionization, even in the presence of salts and in complex mixtures . These authors ascribed the success of the novel matrix vs traditional matrixes to better ablation capability and increased hydrophobicity.…”

Section: Traditional Ionization Methods For Msmentioning

confidence: 99%

Advances in Ionization for Mass Spectrometry

Peacock¹,

Zhang

Trimpin

2016

Anal. Chem.

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Section: Traditional Ionization Methods For Msmentioning

confidence: 99%

Advances in Ionization for Mass Spectrometry

Peacock¹,

Zhang

Trimpin

2016

Anal. Chem.

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“…Numerous studies have been devoted to MALDI sensitivity improvement and ISE alleviation for a wide range of analytes. Previously, the development of a matrix with high salt‐tolerance was reported to alleviate the ISE in protein and peptide analysis . Several studies compared the effects of matrix application techniques on several aspects of MALDI‐MSI performance, including analyte diffusion, reproducibility, and sensitivity that are directly related to the ISE of a MALDI source .…”

Section: Introductionmentioning

confidence: 99%

“…Previously, the development of a matrix with high salt-tolerance was reported to alleviate the ISE in protein and peptide analysis. 25–26 Several studies compared the effects of matrix application techniques on several aspects of MALDI-MSI performance, including analyte diffusion, reproducibility, and sensitivity that are directly related to the ISE of a MALDI source. 27–29 MALDI sensitivity was also reported to be improved through the rational design of matrices and the addition of glycerol which generates multiply-charged protein/peptide ions.…”

Section: Introductionmentioning

confidence: 99%

Characterizing and alleviating ion suppression effects in atmospheric pressure matrix‐assisted laser desorption/ionization

Cao

Liu

et al. 2019

Rapid Comm Mass Spectrometry

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RATIONALE: As a powerful ambient ion source, atmospheric pressure (AP)-MALDI enables direct analysis at atmospheric pressure/temperature and minimal sample preparation. With the increasing usage of AP-MALDI sources with Orbitrap instruments, systematic characterization of the extent of ion suppression effect (ISE) in AP-MALDI-Orbitrap mass spectrometry imaging (MSI) is desirable. Recently, a new low-pressure MALDI platform has been introduced that reportedly provided better sensitivity. While extensive research efforts have been devoted to improving spatial resolution, fewer studies focused on the characterization and sensitivity improvement of these MALDI platforms that, coupled with high-resolution Orbitraps, provide powerful strategy for MS imaging. METHODS: Here, we compared the analytical performance of AP and low-pressure (subatmospheric) MALDI sources to study the effect of pressure control in the ion source. Using a model peptide/protein mixture, we systematically evaluated the factors influencing ISE. Furthermore, the effect of laser spot size was evaluated through tissue imaging analysis of lipids and neuropeptides. The effects of ion suppression and laser spot size have also been examined by comparing the number of identified molecular species during MSI analysis. RESULTS: Several key operating parameters including source pressure, laser energy, laser repetition rate, and microscopic slide coating materials were optimized to minimize the ISE. Under the optimal conditions, the subatmospheric AP-MALDI-Orbitrap platform with high spatial and mass spectral resolution enabled significantly improved coverage of several lipid and neuropeptide families in the MS analysis of mouse brain tissue sections. CONCLUSIONS: The new SubAP-MALDI source coupled with an Orbitrap mass spectrometer was established as a viable platform for in situ endogenous biomolecular analysis with increased sensitivity compared to conventional AP-MALDI sources as evidenced by the confident identification of neuropeptides from mouse brain imaging analyses. The alleviated ISE was key to substantial performance improvement due to optimized intermediate pressure conditions and better ion collection by the ion funnel.

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“…There has been a number of matrices containing α-cyanocinnamic acid (CCA) core units developed for MALDI-MS analyses (Figure A), possibly because of the high performance of the CCA unit in UV-adsorption and energy transfer during ionization of analytes. − Bearing this in mind, we herein rationally designed the reactive matrix PAPAN (Figure A) on the basis of chemical modification of the CCA core unit for sensitive and selective analysis of glycans. The amino group at the R 1 position allows PAPAN to react with the reducing ends of glycans via formation of a Schiff base bond. , The changing of the carboxy group into a phenyl group at the R 2 position may improve the UV absorption efficiency of matrix, which is crucial for improving ionization efficiency .…”

Section: Resultsmentioning

confidence: 99%

2-Phenyl-3-(p-aminophenyl) Acrylonitrile: A Reactive Matrix for Sensitive and Selective Analysis of Glycans by MALDI-MS

Ling

Xiao

et al. 2019

Anal. Chem.

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Analysis of glycans by matrix-assisted laser desorption/ ionization mass spectrometry (MALDI-MS) is usually limited by the intrinsically low abundance and low ionization efficiency of glycans. Aiming to enhance the ionization efficiency of glycans and simplify the sample preparation procedure during MALDI-MS analysis, we reported herein a novel reactive matrix, 2-phenyl-3-(p-aminophenyl) acrylonitrile (PAPAN), for sensitive and selective detection of glycans. PAPAN is a derivative of αcyanocinnamic acid, which possesses high ionization efficiency in MALDI-MS. The PAPAN can react with the terminal aldehyde of glycans and thereby enable the significant enhancement of ionization efficiency of glycans. As a result, using PAPAN as a reactive matrix, the detection sensitivity for glycans was improved 100-fold compared with that using 2,5dihydroxybenzoic acid (DHB) as the matrix. Meanwhile, the ionization of peptides can be significantly suppressed using PAPAN as the matrix, which allowed the selective detection of N-glycans from a deglycosylated tryptic digest of glycoprotein without any prepurification. Moreover, the PAPAN matrix also endowed the analysis of glycans with enhanced fragmentation during MS/MS analysis, which could facilitate glycan structure interpretation. Finally, PAPAN was successfully used for the analysis of N-glycome in human serum. Thus, a simple, sensitive, and selective method for the analysis of glycans has been achieved by using a novel reactive matrix, PAPAN.

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(E)-Propyl α-Cyano-4-Hydroxyl Cinnamylate: A High Sensitive and Salt Tolerant Matrix for Intact Protein Profiling by MALDI Mass Spectrometry

Cited by 21 publications

References 52 publications

Advances in Ionization for Mass Spectrometry

Advances in Ionization for Mass Spectrometry

Characterizing and alleviating ion suppression effects in atmospheric pressure matrix‐assisted laser desorption/ionization

2-Phenyl-3-(p-aminophenyl) Acrylonitrile: A Reactive Matrix for Sensitive and Selective Analysis of Glycans by MALDI-MS

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