Solvent-free MALDI-MS for the Analysis of β-Amyloid
I. Solvent-free based on the mini-ball mill (MBM) method. A general solvent-free protocol was used [4]. Mixing of the analyte and matrix powder was An efficient, low sample load mini-ball mill (MBM) sample preparation procedure was developed for solvent-free MALDI analysis of peptides and proteins. Solvent-free MALDI-MS for the analysis of biological samples via a
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Solvent-free MALDI-MS for the analysis of β-amyloid peptides via
Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ionization (MALDI) analysis of mixtures of β-amyloid peptides (1–11), (33–42), Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ionization (MALDI) analysis of mixtures of beta-amyloid peptides (1-11), (33 Solvent-free MALDI-MS for the analysis of beta-amyloid PubMed
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Solvent-free MALDI-MS for the analysis of biological samples via a mini
A mini ball mill (MBM) solvent-free matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) method allows for the analysis of bacteriorhodopsin (BR), an integral membraneAn efficient, low sample load mini-ball mill (MBM) sample preparation procedure was developed for solvent-free MALDI analysis of peptides and proteins. Picomole sample amounts can be handled conveniently, with 30 s grinding times being sufficient. Matrix purity and molar analyte/matrix ratios are not as critical as with methods Solvent-free MALDI-MS for the analysis of biological samples via a mini
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Solvent-free MALDI-MS for the Analysis of Biological Samples via a Mini
Solvent-Free MALDI-MS Based on the Mini-Ball Mill (MBM) Method A general protocol was developed by adapting existing grinding procedures [5, 8] in order to downscale the method for biologically-relevant analyte amounts (Ta-ble 1). The sample/matrix-ratio was varied, as were other experimental conditions which are depicted by numbers E-1 to E-10Solvent-free MALDI-MS for the analysis of biological samples via a mini-ball mill approach . × Close Log In. Log in with Facebook Log in with Google. or. Email. Password. Remember me on this computer. or reset password. Enter the email address you signed up with and we'll email you aSolvent-free MALDI-MS for the analysis of biological samples via a mini
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Solvent-free MALDI-MS for the analysis of Springer
Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ionization (MALDI) analysis of mixtures of β-amyloid peptides (1–11), (33–42), (1–42) and non-β-amyloid component of Alzheimer’s disease peptide yielded interpretable spectra for all of the peptides present regardless of their relative amounts in An efficient, low sample load mini-ball mill (MBM) sample preparation procedure was developed for solvent-free MALDI analysis of peptides and proteins. Picomole sample amounts can be handled conveniently, with 30 s grinding times being sufficient. Matrix purity and molar analyte/matrix ratios are no Solvent-free MALDI-MS for the analysis of biological samples via a mini
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Investigations of theoretical principles for MALDI-MS derived from
Solvent-free sample preparation. The procedure is described in detail in a previous report [14]. Briefly, the analyte and matrix were simply mixed in the appropriate molar ratio and shaken by a ball mill for homogenization. The powder was crushed on the target as a very fine powder to produce a very thin coverage of the analyte:matrix mixture.A limitation of any current approach using solvent-free MALDI mass spectrometry is that only one sample at a time can be prepared and transferred to the MALDI-plate. S. ; Deinzer, M. L. Solvent-free MALDI-MS for the Analysis of a Membrane Protein via the Mini-Ball Mill Approach: a Case Study of Bacteriorhodopsin. Anal. Multisample preparation methods for the solvent-free MALDI
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Synthesis of Metal Organic Frameworks by Ball-Milling MDPI
In the case of DMF as an auxiliary solvent, under 2.9 g of ball milling conditions, an intermediate phase (2) was formed after about 20 min, and the product of Zn-MOF-74 appeared after about 45 min, and when a heavier 3.5 g ball was used, the above-mentioned time was shortened to 10 and 40 min, respectively.Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ionization (MALDI) analysis of mixtures of beta-amyloid peptides (1-11), (33-42), (1-42) and non-betaSolvent-free MALDI-MS for the Analysis of ??-Amyloid
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Solvent-Free MALDI-MS for the Analysis of a Membrane
Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ionization (MALDI) analysis of mixtures of beta-amyloid peptides (1-11), (33-42), (1-42) and non-betaAbstract. An expedient, mechanochemical, operationally simple protocol is reported for the Rh-catalysed C–H methylation of (hetero)arenes under solvent-free conditions without the use of a ball mill. Reagent mixing and activation are delivered using simple pestle-and-mortar grinding and subsequent heating, providing access to the sameSolvent-free and ball mill-free catalytic C–H methylation
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Solvent-free MALDI-MS: Developmental improvements in the
Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances. Journal of the American Society for Mass Spectrometry 2007,18 (8),1533-1543.The method and clean-up issues related to solvent-free MALDI-MS, which were considered a serious obstacle for routine and high throughput use, can be overcome using recently described solvent-free sample preparation strategies, such as vortexing [41, 42], mini-ball mill [28, 29], and in particular, on-target grinding [42] methods, which can Solvent-Free MALDI-MS: Developmental Improvements in the
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Solvent-Free Ball-Milling Biginelli Reaction by Subcomponent
Reactions were performed under solvent-free, metal-free, mechanochemical (ball milling) and ambient laboratory conditions. Br+-catalyzed oxidation of benzyl alcohols led to the product benzaldehydes and byproduct H+ which were further promoted as component and catalyst, respectively, for a cascade transformation to Solvent-free MALDI-MS proved valuable for the characterization of nanosized material, e.g., fullereno-based structures, which indicated having an increased fragmentation-susceptibility. New analyte/matrix Trimpin, S.; Deinzer, M. L. Solvent-free MALDI-MS for the analysis of biological samples via a mini-ball mill approach. J. Am.Solvent-free MALDI-MS: Developmental improvements in the
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Solvent-free MALDI-MS for the analysis of biological samples via a mini
An efficient, low sample load mini-ball mill (MBM) sample preparation procedure was developed for solvent-free MALDI analysis of peptides and proteins. Picomole sample amounts can be handled conveniently, with 30 s grinding times being sufficient. Matrix purity and molar analyte/matrix ratios are not as critical as with methods vent is not an issue, the solvent-free method is generally less efficient. Workflow and clean-up issues related to solvent-free MALDI analysis were considered serious handicaps for high-throughput applications. These res-ervations are partially overcome by the vortex [6] and mini-ball-mill (MBM) methods [7–9]. An on-targetMultisample preparation methods for the solvent-free MALDI-MS
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Solvent-free MALDI-MS for the analysis of a membrane protein
The solvent-free MALDI-MS method allows for the analysis of bacteriorhodopsin (BR), an integral membrane protein that previously presented special analytical problems, and expands the range of peptides that can be effectively analyzed to those that are hydrophobic and solubility-limited. A mini ball mill (MBM) solvent-free matrix-assisted laser Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ ionization (MALDI) analysis of mixtures of -amyloid peptides (1-11), (33-42), (1-42) and non- -amyloid component of Alzheimer’s disease peptide yielded interpretable spectra for all of the peptides present regardless of their relative amounts in the samples.Solvent-free MALDI-MS for the analysis of <Emphasis Type
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