Comparison of different processing pipelines for dia PASEF ® data
Posters | 2020 | BrukerInstrumentation
The dia-PASEF technique integrates trapped ion mobility spectrometry with data-independent acquisition to enhance ion utilization, specificity, and sensitivity. This improvement supports comprehensive and accurate label-free quantification in complex proteomic samples.
This study evaluates and contrasts multiple computational workflows for processing dia-PASEF datasets. Four main pipelines were assessed: Mobi-DYK/OpenSWATH with MaxQuant, Spectronaut 14 library generation and direct-DIA, and PEAKS Studio X+ with its Pulsar engine.
Complex mixtures of tryptic digests from Arabidopsis thaliana, Yarrowia lipolytica, and Streptomyces coelicolor were prepared in two defined ratios. Spectral libraries were built from eight high-pH fractions analyzed on a Bruker timsTOF Pro using both DDA-PASEF and dia-PASEF acquisition modes. Data processing settings were harmonized across workflows with a 1% FDR threshold at the peptide level.
Each pipeline successfully generated CCS-aware libraries exceeding 10 000 protein groups and 70 000 unique peptides. Library-based approaches achieved over 70% recovery in 90 min runs, while direct-DIA exceeded 55%. All workflows provided accurate quantification ratios, demonstrating robust performance across software platforms. Notably, newer software versions are expected to further improve results, particularly for the Mobi-DYK/OpenSWATH combination.
The incorporation of the ion mobility dimension in the processing workflows enhances selectivity and identification confidence. CCS-aware analysis enables deeper proteome coverage and precise quantitation, supporting applications in systems biology, biomarker discovery, and quality control.
Ongoing software developments and updates will refine library generation and data analysis workflows. Integration of machine learning for spectral prediction, expansion of shared CCS databases, and real-time PASEF acquisition strategies are anticipated to further boost throughput and sensitivity.
All evaluated pipelines reliably support dia-PASEF data analysis and CCS-aware library construction. The choice of processing software may be guided by existing infrastructure and desired quantification depth, with prospects for continued performance gains through software enhancements.
Ion Mobility, LC/TOF, LC/HRMS, LC/MS, LC/MS/MS
IndustriesProteomics
ManufacturerBruker
Summary
Significance of the Topic
The dia-PASEF technique integrates trapped ion mobility spectrometry with data-independent acquisition to enhance ion utilization, specificity, and sensitivity. This improvement supports comprehensive and accurate label-free quantification in complex proteomic samples.
Study Objectives and Overview
This study evaluates and contrasts multiple computational workflows for processing dia-PASEF datasets. Four main pipelines were assessed: Mobi-DYK/OpenSWATH with MaxQuant, Spectronaut 14 library generation and direct-DIA, and PEAKS Studio X+ with its Pulsar engine.
Methodology
Complex mixtures of tryptic digests from Arabidopsis thaliana, Yarrowia lipolytica, and Streptomyces coelicolor were prepared in two defined ratios. Spectral libraries were built from eight high-pH fractions analyzed on a Bruker timsTOF Pro using both DDA-PASEF and dia-PASEF acquisition modes. Data processing settings were harmonized across workflows with a 1% FDR threshold at the peptide level.
Used Instrumentation
- nanoElute nano-HPLC system (Bruker Daltonics)
- 250 mm IonOpticks pulled-emitter column
- timsTOF Pro mass spectrometer (Bruker Daltonics) operated in PASEF and dia-PASEF modes
Key Results and Discussion
Each pipeline successfully generated CCS-aware libraries exceeding 10 000 protein groups and 70 000 unique peptides. Library-based approaches achieved over 70% recovery in 90 min runs, while direct-DIA exceeded 55%. All workflows provided accurate quantification ratios, demonstrating robust performance across software platforms. Notably, newer software versions are expected to further improve results, particularly for the Mobi-DYK/OpenSWATH combination.
Benefits and Practical Applications
The incorporation of the ion mobility dimension in the processing workflows enhances selectivity and identification confidence. CCS-aware analysis enables deeper proteome coverage and precise quantitation, supporting applications in systems biology, biomarker discovery, and quality control.
Future Trends and Potential Applications
Ongoing software developments and updates will refine library generation and data analysis workflows. Integration of machine learning for spectral prediction, expansion of shared CCS databases, and real-time PASEF acquisition strategies are anticipated to further boost throughput and sensitivity.
Conclusion
All evaluated pipelines reliably support dia-PASEF data analysis and CCS-aware library construction. The choice of processing software may be guided by existing infrastructure and desired quantification depth, with prospects for continued performance gains through software enhancements.
References
- Chapelle M., Henry C., Millan-Oropeza A., Schmit P.-O., Kaspar S. Comparison of different processing pipelines for dia-PASEF data. Bruker application note, 2019.
Content was automatically generated from an orignal PDF document using AI and may contain inaccuracies.
Similar PDF
High throughput 4D-Proteomics – Application of dia-PASEF® and the Evosep One for short gradients
2020|Bruker|Applications
High throughput 4D-Proteomics – Application of dia-PASEF® and the Evosep One for short gradients The timsTOF Pro offers a combination of two unique technologies, namely a 4th dimension provided by Trapped Ion Mobility Spectrometry (TIMS) to enhance ion separation and…
Key words
pasef, pasefdia, diaevosep, evoseptimstof, timstofresource, resourcespd, spdmobility, mobilitydata, dataspectronaut, spectronautprecursor, precursorbruker, brukerlibrary, libraryspecific, specificion, iontims
Parallel accumulation – serial fragmentation combined with data-independent acquisition (diaPASEF)
2019|Bruker|Applications
Parallel accumulation – serial fragmentation combined with data-independent acquisition (diaPASEF) The timsTOF Pro with diaPASEF enables deeper proteome coverage in a single 4D shotgun proteomics experiment, with highly reproducible qualitative and quantitative results – making it a near-ideal mass analyzer…
Key words
diapasef, diapasefmobility, mobilitydia, diaion, ionmedian, medianpasef, pasefpeptide, peptideproteins, proteinsdik, dikschemes, schemestims, timspeptides, peptidesplacement, placementduty, dutymobi
diaPASEF: label-free quantification of highly complex proteomes
2019|Bruker|Applications
diaPASEF: label-free quantification of highly complex proteomes The timsTOF Pro with diaPASEF provides reproducible and accurate qualitative and quantitative results in complex proteomics samples – making it perfectly suited for data-independent acquisition approaches. Abstract Data-independent acquisition (DIA) promises reproducible and…
Key words
hye, hyediapasef, diapasefdia, diaspectronaut, spectronauttimstof, timstofpasef, pasefproteomics, proteomicstriply, triplywindows, windowsapproaches, approachesproteomes, proteomesion, ionprotein, proteinpro, proreproducible
dia-PASEF® applied on different gradient lengths
2020|Bruker|Technical notes
dia-PASEF® applied on different gradient lengths Data Independent Acquisition (DIA) workflows have gained in popularity as they overcome the issue of stochastic selection of peptide precursors encountered in typical data-dependent approaches (DDA) and thereby promise reproducible and accurate protein identification…
Key words
pasef, pasefdia, diahela, helayeast, yeastmobility, mobilitycumulative, cumulativeprotein, proteinlibrary, librarycoverage, coveragepeptides, peptideswindows, windowsspectronaut, spectronaution, iontims, timsgroups