Nano-electrospray Source
Nano-electrospray Source - Related Videos
10:47
Whole-body Mass Spectrometry Imaging by Infrared Matrix-assisted Laser Desorption Electrospray Ionization (IR-MALDESI)
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Cited by 19 •
2016
A mass spectrometry imaging (MSI) source operated at atmospheric pressure was developed by coupling mid-infrared laser desorption and electrospray post-ionization. Exogenous ice matrix was used as the energy-absorbing matrix to facilitate resonant desorption of tissue-related material. This manuscript provides a step-by-step protocol for performing IR-MALDESI MSI of whole-body neonatal mouse.
08:38
Electrospray Deposition of Uniform Thickness Ge23Sb7S70 and As40S60 Chalcogenide Glass Films
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Cited by 8 •
2016
A method of uniform thickness solution-derived chalcogenide glass film deposition is demonstrated using computer numerical controlled motion of a single-nozzle electrospray.
04:13
Bioscaffold Fabrication by Electrospraying: A Technique to Generate Microcarrier Scaffolds Derived from Extracellular Matrix of Decellularized Tissue
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2023
This video demonstrates the procedure of extracellular matrix-derived microcarrier fabrication by electrospraying. These microcarriers simulate the native tissue-specific microenvironment and are stable in long-term 3D in vitro cell culture models.
08:43
A Quantitative Assessment of The Yeast Lipidome using Electrospray Ionization Mass Spectrometry
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Cited by 39 •
2009
We describe a new quantitative lipidomics method for identifying numerous lipid species in yeast using survey-scan electrospray ionization mass spectrometry (ESI/MS). This method exceeds currently available methods for lipid identification and quantification in the ability to resolve various molecular forms of lipids, sensitivity, and speed.
11:56
Fluorescence Imaging with One-nanometer Accuracy (FIONA)
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Cited by 11 •
2014
Single fluorophores can be localized with nanometer precision using FIONA. Here a summary of the FIONA technique is reported, and how to carry out FIONA experiments is described.
FAQs
At the emitter tip, the applied high voltage organizes the liquid into a Taylor cone and produces charged droplets. As solvent evaporates, the droplets become less stable and undergo repeated fission, reducing their size. This sequence increases the relative concentration of analyte and supports release of peptide, protein, lipid, or other biomolecular ions for mass analysis.
Low-flow operation limits the amount of biological solution consumed while maintaining efficient transfer of ions into the mass spectrometer. That combination is especially valuable when samples are scarce or when a complex mixture contains analytes at low abundance. The source therefore supports sensitive measurements without requiring large sample volumes.
The fine emitter and applied voltage work together by directing liquid through a small outlet and driving formation of the charged cone and droplet plume. Subsequent solvent evaporation and fission determine how effectively analyte ions are liberated. These linked steps matter because ion release controls how much material becomes available for mass spectrometric detection.
To use a Nano-electrospray Source, a liquid biological sample is delivered through a fine emitter while a high voltage is applied. The resulting charged-droplet plume is directed toward the mass spectrometer, where solvent loss and droplet fission generate gas-phase analyte ions. Consistent delivery and stable plume formation are central to obtaining usable measurements.
A Nano-electrospray Source supports proteomics, metabolomics, and the characterization of biological molecules from limited samples. In these applications, mass spectrometric analysis can address peptides, proteins, lipids, and other biomolecules. Its low sample consumption makes the approach relevant when available biological material is restricted but molecular measurement remains necessary.
Efficient ion transfer from low-flow samples can improve detection of components within complex biological mixtures. The resulting mass spectrometric data support characterization of peptides, proteins, lipids, and other biomolecules, while molecular identification helps distinguish analyzed components. This combination is particularly useful when limited sample quantities must support detailed biological measurement.