High mass selectivity for top-down proteomics by application of SWIFT technology

Area of Science:

• Analytical Chemistry
• Biochemistry
• Spectrometry

Background:

• Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry is a powerful analytical technique.
• Stored waveform inverse Fourier transform (SWIFT) offers advanced ion manipulation capabilities.
• Characterizing intact proteins requires high-resolution mass analysis and selective ion isolation.

Purpose of the Study:

• To implement SWIFT technology on a commercial FT-ICR mass spectrometer.
• To evaluate the mass selectivity and ion isolation capabilities of SWIFT for intact proteins.
• To demonstrate the utility of SWIFT-enabled top-down analysis for protein characterization.

Main Methods:

• Implementation of SWIFT using an arbitrary waveform generator (AWG) and high-speed analog switch.
• Generation of complex ejection/isolation waveforms for selective ion manipulation.
• Analysis of intact Bovine histone H4 using SWIFT isolation followed by electron capture dissociation (ECD).

Main Results:

• Successful implementation of SWIFT on a commercial FT-ICR mass spectrometer.
• Achieved high mass selectivity of approximately 0.1 m/z unit for isolating specific charge states (18+).
• Demonstrated successful electron capture dissociation (ECD) of SWIFT-isolated Bovine histone H4 ions.

Conclusions:

• SWIFT technology can be effectively adapted to commercial FT-ICR mass spectrometers.
• SWIFT provides enhanced capabilities for high-mass-selectivity ion isolation in top-down proteomics.
• This approach improves the characterization of intact proteins through detailed top-down analysis.