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A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues
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A Reproducible Multichannel Synchronous Rapid Phosphopeptide Enrichment Strategy Enabled by Anisotropic Porous

Qian Liu1,2,3, Dandan Zhou4, Kenan Wang1

  • 1College of Chemistry and Material Science, Northwest University, Xi'an 710127, China.

Analytical Chemistry
|May 29, 2026
PubMed
Summary

A novel anisotropic porous monolith enables rapid, high-throughput phosphopeptide enrichment from complex biosamples. This multichannel synchronous rapid enrichment (MCSR) strategy significantly reduces processing time and enhances proteomic analysis for tumor biomarker discovery.

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Preparation of Highly Porous Coordination Polymer Coatings on Macroporous Polymer Monoliths for Enhanced Enrichment of Phosphopeptides

Published on: July 14, 2015

Area of Science:

  • Proteomics
  • Analytical Chemistry
  • Biomaterials

Background:

  • Large-scale protein phosphorylation analysis is crucial for identifying tumor biomarkers and drug targets.
  • Current methods face challenges due to complex sample processing and batch variations.
  • High-throughput analytical methods are needed for efficient analysis of clinical samples.

Purpose of the Study:

  • To develop a high-throughput analytical method for complex biosamples using an anisotropic porous monolith.
  • To establish a rapid phosphopeptide enrichment strategy overcoming limitations of traditional methods.
  • To demonstrate the potential of the developed method in clinical proteomics research.

Main Methods:

  • Fabrication of an anisotropic porous monolith (CS-ZrPC@PLP) using directional freeze-casting.
  • Development of a multichannel synchronous rapid enrichment (MCSR) strategy utilizing the monolith.
  • Application of MCSR for simultaneous phosphopeptide enrichment of multiple complex biological samples.

Main Results:

  • The MCSR strategy achieved rapid enrichment (5 min) of phosphopeptides from eight sample sets, including cell lysates.
  • Demonstrated high selectivity for phosphopeptides with minimal interference from abundant proteins like BSA.
  • Identified 41,626 phosphopeptides and 7,168 phosphoproteins from Hep G2 cell digests using microflow LC-MS/MS after rapid enrichment.

Conclusions:

  • The developed anisotropic porous monolith and MCSR strategy offer a significant advancement in high-throughput phosphopeptide enrichment.
  • This method overcomes traditional bottlenecks, enabling faster and more efficient proteomic analysis.
  • The strategy shows great potential for clinical proteomics, facilitating biomarker discovery and drug target identification.