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Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
Published on: February 27, 2020
Synthetic plasma pool cohort correction for affinity-based proteomics datasets allows multiple study comparison
Dries Heylen1,2, Murih Pusparum2,3, Jurgis Kuliesius4
1Data Science Institute, Theory Lab, Hasselt University, 3590 Diepenbeek, Belgium.
Quantitative proteomics using OLINK Target 96 enables disease research. A new Synthetic Plasma Pool Cohort Correction (SPOC) method allows accurate, cost-efficient data comparison across studies without resending samples.
Area of Science:
- Proteomics
- Genomics
- Biotechnology
Background:
- Quantitative proteomics links genomics to human diseases by analyzing protein levels.
- OLINK's Target 96 is a prominent affinity-based protein measurement method used in large cohorts like SCALLOP.
- Current methods for comparing OLINK Target 96 data across independent cohorts are logistically challenging and costly.
Purpose of the Study:
- To develop a robust and cost-efficient method for accurate quantitative comparison of OLINK Target 96 protein data across independent studies.
- To address the limitations of the 'biological bridging sample' approach in multi-cohort proteomics collaborations.
Main Methods:
- Development of the Synthetic Plasma Pool Cohort Correction (SPOC) approach.
- Utilizing an OLINK-composed synthetic plasma sample for normalization.
- Implementation in a federated data-sharing context, demonstrated with a sepsis use case.
Main Results:
- The SPOC correction method provides accurate and cost-efficient normalization for OLINK Target 96 data.
- The approach simplifies multi-cohort data comparison, overcoming logistical hurdles.
- Successful illustration of the method's utility in a sepsis research scenario.
Conclusions:
- The SPOC correction offers a practical solution for inter-cohort comparison of proteomics data.
- This method enhances collaboration and data sharing in large-scale proteomics studies.
- SPOC correction facilitates more accessible and efficient proteomic data analysis across diverse research settings.
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