Nanoparticle Enrichment of Volumetrically Accurate Microsampled Blood for Enhanced Proteomic Analysis of Dried Blood
- Jul 16
- 2 min read
Updated: 3 days ago
Presentation: Campbell et al., Cedars-Sinai Medical Center, ASMS 2026 Poster
Overview
This study evaluated the performance of the Nanotrap® Protein Enrichment Affinity Kit (PEAK) for high-throughput proteomic analysis of volumetrically accurate dried blood spot (VDBS) samples. The investigators developed and optimized a plate-based, single-day workflow for both plasma and dried blood and compared its performance with other proteomic sample preparation methods. The goal was to determine whether Nanotrap PEAK could provide a scalable, reproducible, and cost-effective alternative for large clinical proteomics studies while maintaining strong proteome depth and analytical precision.
Key Findings
Robust proteome coverage with a scalable workflow
The optimized Nanotrap PEAK workflow enabled comprehensive proteomic profiling from both plasma and VDBS using a single-day, plate-based protocol compatible with high-throughput clinical studies.
A shortened 2-hour digestion protocol (37°C; TEAB or Tris+CaCl₂ buffer) maintained protein depth and analytical precision while reducing sample preparation time by approximately 50%.
Strong performance in dried blood samples
The Ceres R&D Nanotrap workflow outperformed the commercial workflow for VDBS samples, while the commercial workflow remained optimal for plasma.
VDBS shared more than 60% of identified proteins with matched plasma samples, and more than half of VDBS proteins achieved intra-assay CVs below 20%, demonstrating strong analytical performance despite the increased complexity of whole blood.
Excellent reproducibility
Across three independently prepared experimental days, more than 80% of proteins were consistently detected.
Over 60% of proteins exhibited inter-day CVs below 20% in both plasma and VDBS, supporting robust reproducibility for longitudinal and large-cohort studies.
Plasma and VDBS protein abundances showed strong agreement (Pearson r = 0.86) for low-variability proteins, supporting quantitative comparisons across sample types.
Biological relevance demonstrated
The optimized workflow detected 25 of 31 curated Alzheimer's disease-associated proteins, including several brain-enriched proteins.
Six Alzheimer's-related proteins were detected exclusively in VDBS, largely representing complement and coagulation pathway proteins.
In an independent heart disease cohort of 115 participants, the VDBS workflow consistently quantified more than 2,500 proteins, demonstrating suitability for large clinical studies.
Implications for Nanotrap Technology
This study demonstrates that Nanotrap PEAK enables high-quality, discovery-scale proteomics from microsampled dried blood, extending deep proteomic analysis beyond conventional plasma workflows. The optimized workflow combines strong proteome coverage, high reproducibility, rapid sample processing, and compatibility with automated, plate-based formats, making it well suited for large population studies, decentralized sample collection, and precision medicine applications where dried blood sampling offers logistical advantages.
Conclusion
The authors conclude that while the Seer Proteograph platform remains the benchmark for maximum proteome depth, Nanotrap PEAK provides a compelling cost-effective alternative for both plasma and dried blood proteomics. Its optimized 2-hour, single-day workflow delivers robust reproducibility, strong cross-matrix concordance, and biologically meaningful protein detection, establishing Nanotrap PEAK as a scalable platform for high-throughput clinical proteomics and biomarker discovery.
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