Protein aggregation capture on microparticles enables multi-purpose proteomics sample preparation

Research output: Contribution to journalJournal articleResearchpeer-review

Universal proteomics sample preparation is challenging due to the high heterogeneity of biological samples. Here we describe a novel mechanism that exploits the inherent instability of denatured proteins for non-specific immobilization on microparticles by protein aggregation capture. To demonstrate the general applicability of this mechanism, we analyzed phosphoproteomes, tissue proteomes, and interaction proteomes as well as dilute secretomes. The findings presents a practical, sensitive and cost-effective proteomics sample preparation method.

Original languageEnglish
JournalMolecular and Cellular Proteomics
Publication statusE-pub ahead of print - 4 Mar 2019

Bibliographical note

Published under license by The American Society for Biochemistry and Molecular Biology, Inc.

ID: 214465266