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Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

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Mass spectrometry is an analytical technique used to determine the molecular mass and molecular formula of a compound. The basic principle of mass spectrometry is to generate ions from the analyte molecule and measure these ion abundances against their molecular mass. One common type of ionization, known as electron ionization or EI, bombards the analyte molecules in the gas phase with high-energy electron beams. The electron beams displace an electron from the molecule and leave behind a...
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Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

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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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In mass spectroscopy, amines undergo fragmentation to give parent ions with odd molecule weights. This observed mass spectrum follows the nitrogen rule; a molecule with an odd number of nitrogen atoms produces a molecular ion with an odd molecular weight. Amines undergo fragmentation through α cleavage, producing nitrogen-containing cations—iminium ions—and alkyl radicals. Mass spectra of aromatic and cyclic aliphatic amines exhibit strong molecular ion peaks, but acyclic...
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Mass Spectrometry: Isotope Effect01:13

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Most elements exist in nature as a mixture of isotopes. The isotopes differ in weight due to their respective number of neutrons. The molecular weight of a molecule is different depending on the specific isotope of its elements involved. As a result, the mass spectrum of the molecule exhibits peaks from the same fragment at multiple positions. The positions of these mass signals depend on the mass differences between isotopes. Furthermore, the intensity of these signals is dependent on the...
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Chemical Ionization (CI) Mass Spectrometry01:21

Chemical Ionization (CI) Mass Spectrometry

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The molecular ion peak of a molecule in the mass spectrum provides vital information for molecular identification. However, conventional electron impact ionization can lead to the rapid dissociation of some molecular ions before they reach the detector. A milder ionization method is required to increase the lifetime of such ionized analyte molecules. Chemical ionization (CI) is a gas-phase protonation reaction useful for mass-analyzing analyte molecules that are easily protonated to yield the...
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Mass Spectrometry: Alkene Fragmentation00:59

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Alkenes lose one electron from the unsaturated π bond upon ionization and form stable molecular ions. Further fragmentation of alkenes occurs through three different reaction pathways. The most prominent fragmentation is the cleavage at the allylic position. The resultant allylic carbocation is resonance stabilized. In the mass spectra of terminal alkenes, this fragment appears at a mass-to-charge ratio of 41. In the internal alkenes, where there are two choices of allylic cleavage, the...
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Semi-Quantitative Analysis of Peptidoglycan by Liquid Chromatography Mass Spectrometry and Bioinformatics
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High-Throughput, Fast, and Sensitive Immunopeptidomics Sample Processing for Mass Spectrometry.

Fabio Marino1,2, Chloe Chong1,2, Justine Michaux1,2

  • 1Ludwig Centre for Cancer Research, University of Lausanne, Epalinges, Switzerland.

Methods in Molecular Biology (Clifton, N.J.)
|January 23, 2019
PubMed
Summary
This summary is machine-generated.

A new protocol enables high-throughput recovery of HLA class I and II peptides for T cell therapy development. This method is sensitive, reproducible, and reduces sample handling for faster analysis.

Keywords:
Affinity purificationAntigen processing and presentationHLA class I and HLA class IIHuman leukocyte antigenImmunopeptidomicsMass spectrometry

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Area of Science:

  • Immunology
  • Proteomics
  • Therapeutic Development

Background:

  • Understanding HLA-presented peptides is vital for cancer and disease therapeutics.
  • Current peptide recovery methods limit mass spectrometry-based analysis.
  • A need exists for efficient and scalable HLA peptide isolation techniques.

Purpose of the Study:

  • To describe a detailed protocol for high-throughput immunoaffinity-purification of HLA class I and class II peptides.
  • To provide a sensitive and reproducible method for peptide recovery from multiple samples.
  • To simplify the pipeline for basic and clinical applications.

Main Methods:

  • Immunoaffinity-purification of HLA-I and HLA-II peptides using a plate format.
  • High-throughput processing of up to 96 samples.
  • Reduced sample handling and rapid protocol completion within 5 hours.

Main Results:

  • A sensitive and reproducible method for HLA peptide recovery was established.
  • The protocol is suitable for both tissue samples and cell lines.
  • Competitive peptide yield was achieved with reduced sample handling.

Conclusions:

  • The developed protocol offers a significant improvement for HLA peptide analysis.
  • This simplified pipeline facilitates innovative therapeutic design for various diseases.
  • The method is applicable to both fundamental research and clinical settings.