Thin-Layer Matrix Sublimation with Vapor-Sorption Induced Co-Crystallization for Sensitive and Reproducible SAMDI-TOF MS Analysis of Protein Biosensors

Roth, Michael J.; Kim, Jaekuk; Maresh, Erica M.; Plymire, Daniel A.; Corbett, J. R.; Zhang, Junmei; Patrie, Steven M.

doi:10.1007/s13361-012-0442-7

Cited by 12 publications

(21 citation statements)

References 56 publications

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“…15 The latter is able to probe different surfaces, which recently opened up new perspectives in the molecular identification of SAMs, 17 nanoparticles, 18 biosensors, 19 and biochips. 20 Actually, the combination of surface MALDI-MS and SAMs on gold evolved in a technique termed by Mrksich as SAMDI.…”

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confidence: 99%

Ambient Surface Analysis of Organic Monolayers using Direct Analysis in Real Time Orbitrap Mass Spectrometry

et al. 2014

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A better characterization of nanometer-thick organic layers (monolayers) as used for engineering surface properties, biosensing, nanomedicine, and smart materials will widen their application. The aim of this study was to develop direct analysis in real time high-resolution mass spectrometry (DART-HRMS) into a new and complementary analytical tool for characterizing organic monolayers. To assess the scope and formulate general interpretation rules, DART-HRMS was used to analyze a diverse set of monolayers having different chemistries (amides, esters, amines, acids, alcohols, alkanes, ethers, thioethers, polymers, sugars) on five different substrates (Si, Si3N4, glass, Al2O3, Au). The substrate did not play a major role except in the case of gold, for which breaking of the weak Au-S bond that tethers the monolayer to the surface, was observed. For monolayers with stronger covalent interfacial bonds, fragmentation around terminal groups was found. For ester and amide-terminated monolayers, in situ hydrolysis during DART resulted in the detection of ions characteristic of the terminal groups (alcohol, amine, carboxylic acid). For ether and thioether-terminated layers, scission of C-O or C-S bonds also led to the release of the terminal part of the monolayer in a predictable manner. Only the spectra of alkane monolayers could not be interpreted. DART-HRMS allowed for the analysis of and distinction between monolayers containing biologically relevant mono or disaccharides. Overall, DART-HRMS is a promising surface analysis technique that combines detailed structural information on nanomaterials and ultrathin films with fast analyses under ambient conditions.

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confidence: 99%

Ambient Surface Analysis of Organic Monolayers using Direct Analysis in Real Time Orbitrap Mass Spectrometry

et al. 2014

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“…Here, we studied the influence of MeCN content in analyte/matrix solutions on sensitive detection of peptides by MALDI‐MS. The solubility of CHCA is heavily dependent on the solvent, with the solubility ranging from 850 mg/mL in dimethylsulfoxide to 0.2 mg/mL in water . To investigate the influence of the MeCN content of CHCA solution on the detection sensitivity, we set the concentration at 0.1 mg/mL, which was well below the reported 0.2 mg/mL, in order to avoid unexpected recrystallization induced when mixing with analyte solution and when contacting with the surface of the target plate.…”

Section: Resultsmentioning

confidence: 99%

“…For MALDI‐TOF MS, sample/matrix application techniques and preparation conditions such as solvent, matrix amount and temperature significantly influence the sensitivity, and a variety of the techniques and conditions have been developed . The most widely used among the techniques is the dried‐droplet (Karas–Hillenkamp) method, which was the original sample application method described in the earliest publications about MALDI‐MS.…”

Section: Introductionmentioning

confidence: 99%

An improved sample preparation method for the sensitive detection of peptides by MALDI‐MS

et al. 2013

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We describe here an optimization study of the sample preparation conditions for sensitive detection of peptides by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). Among many factors in the conditions, we varied the percent acetonitrile in the peptide solution, the percent acetonitrile in the matrix solution and the α-cyano-4-hydroxycinnamic acid (CHCA) concentration in the matrix solution. CHCA was chosen because it is the most frequently used matrix for analyzing peptides. The well-established dried-droplet method was employed for sample deposition. The examined range of the concentration of CHCA was from 0.01 to 10 mg/ml, and the MeCN content of the solvent for matrix/analyte was 10% to 50%. The indicator for the detection sensitivity was the S/N ratio of the peaks of peptides used. Highly increased sensitivity (100- to 1000-fold) was observed for the optimal CHCA concentration of 0.1 mg/ml in 20% MeCN/0.1% aq. trifluoroacetic acid (TFA), as compared with the conventional concentration (10 mg/ml) in 50% MeCN/0.1% aq. TFA. For example, the limit of detection of human ACTH 18-39 was 10 amol/well for the optimal condition but 10 fmol/well for the conventional condition. The optimal condition (0.1 mg/ml CHCA in 20% MeCN/0.1% aq. TFA) was verified with five model peptides and provided significant improvement in sensitivity (by two to three orders of magnitude) compared with the conventional conditions. Optimizing the CHCA concentration and solvent composition significantly improved the detection sensitivity in the analysis of peptides by MALDI-MS.

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“…Many studies have reported that traditional optical detection methods can be replaced by MS for the screening of protein or small molecule microarrays [17,18]. This can avoid false positive results and directly provides molecular information about the analytes.…”

Section: Electronic Supplementary Materialsmentioning

confidence: 99%

Screening of the Binding of Small Molecules to Proteins by Desorption Electrospray Ionization Mass Spectrometry Combined with Protein Microarray

Yao

Wang

Zhang

et al. 2015

J. Am. Soc. Mass Spectrom.

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Abstract. The interaction between bioactive small molecule ligands and proteins is one of the important research areas in proteomics. Herein, a simple and rapid method is established to screen small ligands that bind to proteins. We designed an agarose slide to immobilize different proteins. The protein microarrays were allowed to interact with different small ligands, and after washing, the microarrays were screened by desorption electrospray ionization mass spectrometry (DESI MS). This method can be applied to screen specific protein binding ligands and was shown for seven proteins and 34 known ligands for these proteins. In addition, a high-throughput screening was achieved, with the analysis requiring approximately 4 s for one sample spot. We then applied this method to determine the binding between the important protein matrix metalloproteinase-9 (MMP-9) and 88 small compounds. The molecular docking results confirmed the MS results, demonstrating that this method is suitable for the rapid and accurate screening of ligands binding to proteins.

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Thin-Layer Matrix Sublimation with Vapor-Sorption Induced Co-Crystallization for Sensitive and Reproducible SAMDI-TOF MS Analysis of Protein Biosensors

Cited by 12 publications

References 56 publications

Ambient Surface Analysis of Organic Monolayers using Direct Analysis in Real Time Orbitrap Mass Spectrometry

Ambient Surface Analysis of Organic Monolayers using Direct Analysis in Real Time Orbitrap Mass Spectrometry

An improved sample preparation method for the sensitive detection of peptides by MALDI‐MS

Screening of the Binding of Small Molecules to Proteins by Desorption Electrospray Ionization Mass Spectrometry Combined with Protein Microarray

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