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New split lens devices enable surface-induced dissociation (SID) of proteins and protein complexes. These simpler, smaller devices improve sensitivity and maintain performance across multiple mass spectrometry platforms.

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Area of Science:

  • Mass Spectrometry
  • Proteomics
  • Biophysical Chemistry

Background:

  • Surface-induced dissociation (SID) is a crucial technique for protein analysis.
  • Existing SID devices can be complex and instrument-specific.
  • There is a need for versatile and user-friendly SID technologies.

Purpose of the Study:

  • To develop and evaluate novel, simplified split lens devices for SID.
  • To demonstrate the compatibility and performance of these devices across different mass spectrometry platforms.
  • To showcase the combined capabilities of SID with high-resolution mass spectrometry and ion mobility.

Main Methods:

  • Fabrication of novel split lens geometries for SID.
  • Integration of split lenses into Bruker FT-ICR, Waters Q-IM-TOF, and Thermo Scientific EMR Orbitrap instruments.
  • Characterization of SID performance across a range of protein and protein complex samples.
  • Coupling SID with ion mobility and high-resolution mass spectrometry.

Main Results:

  • The novel split lens devices are minimally invasive and easy to operate.
  • Improved sensitivity was observed in various cases across all tested instrument platforms.
  • Consistent SID capabilities were maintained over a wide mass and energy range.
  • Successful demonstration of SID coupled with ion mobility for diverse protein complexes.

Conclusions:

  • The developed split lens devices offer a simplified and effective approach to SID.
  • These devices enhance sensitivity and maintain performance across multiple mass spectrometry platforms.
  • The technology enables advanced analysis of protein complexes using combined SID, high-resolution MS, and ion mobility.