Protein aggregation capture on microparticles enables multi-purpose proteomics sample preparation
Research output: Contribution to journal › Journal article › Research › peer-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.
|Journal||Molecular and Cellular Proteomics|
|Publication status||E-pub ahead of print - 4 Mar 2019|
Published under license by The American Society for Biochemistry and Molecular Biology, Inc.