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A broad-based study on hyphenating new ionization technologies with MS/MS for PTMs and tissue characterization.

Darrell D Marshall1, Ellen D Inutan1, Beixi Wang1

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Matrix-assisted ionization (MAI) and Laserspray ionization (LSI) enable direct surface analysis of peptides and proteins. These methods, coupled with collision-induced dissociation (CID) and electron transfer dissociation (ETD), provide detailed characterization, including posttranslational modifications.

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Area of Science:

  • Analytical Chemistry
  • Biochemistry
  • Mass Spectrometry

Background:

  • Matrix-assisted ionization (MAI) is a novel technique for generating gas-phase ions from solid samples.
  • Laserspray ionization (LSI) is a specialized form of MAI offering high spatial resolution without direct laser involvement in ionization.
  • Both MAI and LSI produce multiply-charged ions suitable for direct surface characterization.

Purpose of the Study:

  • To evaluate the utility of MAI and LSI coupled with CID and ETD for peptide and protein characterization.
  • To compare MAI/LSI performance against established techniques like electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI).
  • To assess the capability of these methods for analyzing intact proteins and tissue samples.

Main Methods:

  • Utilized several MAI and LSI matrices for peptide and protein analysis.
  • Employed collision-induced dissociation (CID) and electron transfer dissociation (ETD) in conjunction with mass spectrometry.
  • Analyzed intact proteins and protein digests directly from mouse brain tissue sections.
  • Tested the methods on mass spectrometers from two different manufacturers.

Main Results:

  • MAI and LSI, when combined with CID/ETD, yielded characterization information comparable to ESI for most analyses.
  • These methods proved superior to MALDI for intact proteins and protein digests from tissue sections.
  • The soft ionization nature of MAI/LSI facilitated the determination of posttranslational modification sites, such as phosphorylation.
  • Failures in ETD/CID with MAI were linked to insufficient desolvation of charged matrix:analyte particles.

Conclusions:

  • MAI and LSI are effective techniques for direct surface analysis and characterization of peptides and proteins.
  • The combination with CID and ETD expands their utility, particularly for identifying posttranslational modifications.
  • Efficient matrix desolvation is critical for successful tandem mass spectrometry experiments using MAI/LSI.