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Related Concept Videos

Electrospray Ionization (ESI) Mass Spectrometry01:12

Electrospray Ionization (ESI) Mass Spectrometry

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Higher molecular weight biomolecules are nonvolatile compounds that may decompose before ionizing or vaporizing during mass analysis with conventional electron impact ionization methods. Accordingly, electrospray ionization (ESI) is the favored method for vaporizing and ionizing biomolecules as it circumvents rapid fragmentation and enables the recording of mass signals for the entire biomolecule.
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An unknown compound can be established by identifying the molecular ion peak in the mass spectrum. The molecular ion peak is often weak or absent due to the predominance of fragmentation in high-energy electron beams. In such cases, a soft-energy electron beam can be used to scan the spectrum to enhance the intensity of the molecular ion peak. Additionally, chemical ionization, field ionization, and desorption ionization spectra are used to obtain a relatively intense molecular ion peak.To...
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Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
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Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...
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Matrix-assisted laser desorption ionization (MALDI) is a powerful analytical technique used in mass spectrometry. It enables the identification and characterization of various biomolecules, including proteins, peptides, nucleic acids, and carbohydrates. MALDI is an ionization technique, widely employed in biological and medical research, as well as in fields like pharmacology and biochemistry.The analyte of interest, a biomolecule or a mixture of biomolecules, is mixed with a suitable matrix...
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Peptide Identification Using Tandem Mass Spectrometry01:33

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Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
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Imaging of Biological Tissues by Desorption Electrospray Ionization Mass Spectrometry
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Synchronized Desorption Electrospray Ionization Mass Spectrometry Imaging.

Troy J Comi1, Seung Woo Ryu1, Richard H Perry1

  • 1Department of Chemistry, University of Illinois , Urbana, Illinois 61801, United States.

Analytical Chemistry
|November 17, 2015
PubMed
Summary

Synchronization of Desorption Electrospray Ionization (DESI) with mass spectrometer ion injection periods (IT) enhances sensitivity and spatial resolution for ambient mass spectrometry imaging. This optimized sDESI-MSI technique improves analysis of weakly bound analytes on various surfaces.

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Area of Science:

  • Analytical Chemistry
  • Mass Spectrometry Imaging
  • Surface Science

Background:

  • Desorption electrospray ionization (DESI) is a key ambient technique for mass spectral analysis and imaging.
  • Synchronizing DESI with low-duty cycle mass spectrometer ion injection periods (IT) can improve sensitivity and reduce sample depletion.
  • Previous work demonstrated potential benefits of synchronized DESI (sDESI).

Purpose of the Study:

  • To develop and characterize a synchronized DESI mass spectrometry imaging source (sDESI-MSI).
  • To evaluate the impact of sDESI on spatial resolution and sensitivity for analyzing low-intensity analytes.
  • To understand the mechanisms behind performance improvements using simulations.

Main Methods:

  • Development and implementation of an sDESI-MSI source.
  • Characterization of sDESI-MSI performance on an LTQ Orbitrap-XL mass spectrometer.
  • Utilizing computational simulations to model analyte movement and the 'washing effect' during DESI.

Main Results:

  • Synchronization of DESI with IT improved spatial resolution by approximately 4-6 times.
  • sDESI enabled distinct MS imaging of low-intensity endogenous fatty acids in fingermarks at high sampling frequencies (≤ 75 μm step sizes).
  • Simulations confirmed that synchronization reduces the 'washing effect', improving performance, especially for weakly attached analytes.

Conclusions:

  • The sDESI-MSI source significantly enhances spatial resolution and sensitivity in ambient mass spectrometry imaging.
  • Synchronization is crucial for analyzing low-intensity, weakly bound analytes, expanding DESI-MSI applicability.
  • Performance gains are dependent on spray, sample, and surface properties, with the 'washing effect' being a critical factor.