IMSC: Development of an All-Recombinant Intact Protein Standard for LC-MS Application Development and System Suitability Testing
Posters | 2016 | Thermo Fisher ScientificInstrumentation
Advances in liquid chromatography–mass spectrometry (LC-MS) have enabled direct analysis of intact proteins, driving the need for robust quality control (QC) standards. Reliable intact protein benchmarks help laboratories normalize performance, optimize methods, and support top-down proteomics in research, biomanufacturing, and clinical environments.
Seven candidate proteins were purchased or expressed in Escherichia coli and Bacillus subtilis, purified by multi-step protocols including chromatography, dialysis, and desalting. Quality attributes—molecular weight, charge state distribution, purity, and stability—were assessed by:
The original R&D mixture contained seven proteins (cytochrome c, RNase A, myoglobin, trypsin inhibitor, carbonic anhydrase, enolase, BSA) evenly spanning 12–66 kDa. Infusion MS at 140 k resolution demonstrated clear, adduct-free spectra, while 8 k resolution confirmed detection of all components. Recombinant candidates matched the R&D profiles and passed stability tests after lyophilization and storage at –20 °C. UV-HPLC separations on ProSwift™ RP-4H columns yielded distinct peaks for each protein, demonstrating strong chromatographic performance. MS/MS fragmentation and ProSightPC™ results validated sequence identity across the panel.
The all-recombinant standard offers:
As top-down proteomics matures, comprehensive multi-protein standards will be essential for quantitative workflows, biomarker discovery, and biopharmaceutical characterization. Future efforts may incorporate post-translational modifications, antibody standards, and integrated multi-omics QC panels. Integration with automated LIMS and AI-driven data analysis will further streamline QC protocols.
A novel, fully recombinant intact protein mixture was developed and validated for LC-MS and LC-MS/MS QC. This standard meets purity, stability, and reproducibility requirements across a broad molecular weight and m/z range, enabling reliable top-down proteomics and regulatory compliance.
No literature citations provided in the source document.
Consumables, LC/HRMS, LC/MS, LC/MS/MS, LC/Orbitrap
IndustriesProteomics
ManufacturerThermo Fisher Scientific
Summary
Importance of Topic
Advances in liquid chromatography–mass spectrometry (LC-MS) have enabled direct analysis of intact proteins, driving the need for robust quality control (QC) standards. Reliable intact protein benchmarks help laboratories normalize performance, optimize methods, and support top-down proteomics in research, biomanufacturing, and clinical environments.
Objectives and Study Overview
- Develop a stable, high-purity recombinant intact protein mixture covering a broad molecular weight (12–66 kDa) and m/z range (500–2000).
- Ensure reproducibility and compatibility with LC, LC-MS, and LC-MS/MS workflows.
- Replace animal-origin components with fully recombinant proteins for regulatory compliance.
Methodology and Used Instrumentation
Seven candidate proteins were purchased or expressed in Escherichia coli and Bacillus subtilis, purified by multi-step protocols including chromatography, dialysis, and desalting. Quality attributes—molecular weight, charge state distribution, purity, and stability—were assessed by:
- Direct infusion ESI-MS and LC-MS on Thermo Scientific Q Exactive™ hybrid quadrupole-Orbitrap™.
- High-resolution MS/MS (HCD) on Q Exactive HF and Orbitrap Fusion™ Lumos™ Tribrid™ instruments.
- UV-HPLC and SDS-PAGE for chromatographic and integrity checks.
- Data processing with Thermo Scientific ProSightPC™ and Protein Deconvolution™ software.
Main Results and Discussion
The original R&D mixture contained seven proteins (cytochrome c, RNase A, myoglobin, trypsin inhibitor, carbonic anhydrase, enolase, BSA) evenly spanning 12–66 kDa. Infusion MS at 140 k resolution demonstrated clear, adduct-free spectra, while 8 k resolution confirmed detection of all components. Recombinant candidates matched the R&D profiles and passed stability tests after lyophilization and storage at –20 °C. UV-HPLC separations on ProSwift™ RP-4H columns yielded distinct peaks for each protein, demonstrating strong chromatographic performance. MS/MS fragmentation and ProSightPC™ results validated sequence identity across the panel.
Benefits and Practical Applications
The all-recombinant standard offers:
- Animal-origin-free composition for regulatory and clinical labs.
- Broad m/z and MW coverage for method development and instrument calibration.
- High reproducibility supporting day-to-day QC and cross-laboratory harmonization.
Future Trends and Possibilities
As top-down proteomics matures, comprehensive multi-protein standards will be essential for quantitative workflows, biomarker discovery, and biopharmaceutical characterization. Future efforts may incorporate post-translational modifications, antibody standards, and integrated multi-omics QC panels. Integration with automated LIMS and AI-driven data analysis will further streamline QC protocols.
Conclusion
A novel, fully recombinant intact protein mixture was developed and validated for LC-MS and LC-MS/MS QC. This standard meets purity, stability, and reproducibility requirements across a broad molecular weight and m/z range, enabling reliable top-down proteomics and regulatory compliance.
References
No literature citations provided in the source document.
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