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Protein Aggregation Capture on Microparticles Enables Multipurpose Proteomics Sample Preparation.

ABSTRACT: Universal proteomics sample preparation is challenging because of the high heterogeneity of biological samples. Here we describe a novel mechanism that exploits the inherent instability of denatured proteins for nonspecific 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 present a practical, sensitive and cost-effective proteomics sample preparation method.

SUBMITTER: Batth TS

PROVIDER: S-EPMC6495262 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature

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Protein Aggregation Capture on Microparticles Enables Multipurpose Proteomics Sample Preparation.

Batth Tanveer S TS Tollenaere MaximA X MX Rüther Patrick P Gonzalez-Franquesa Alba A Prabhakar Bhargav S BS Bekker-Jensen Simon S Deshmukh Atul S AS Olsen Jesper V JV

Molecular & cellular proteomics : MCP 20190304 5

Universal proteomics sample preparation is challenging because of the high heterogeneity of biological samples. Here we describe a novel mechanism that exploits the inherent instability of denatured proteins for nonspecific 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 present a practical, sensitive and ...[more]

PMID: 30833379

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