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

Tanveer Singh Batth; Maxim A. X. Tollenaere; Patrick Leopold Rüther; Alba Gonzalez-Franquesa; Bhargav Saligram Prabhakar; Simon Holst Bekker-Jensen; Atul Shahaji Deshmukh; Jesper V. Olsen

doi:10.1074/mcp.TIR118.001270

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

Tanveer Singh Batth, Maxim A. X. Tollenaere, Patrick Leopold Rüther, Alba Gonzalez-Franquesa, Bhargav Saligram Prabhakar, Simon Holst Bekker-Jensen, Atul Shahaji Deshmukh, Jesper V. Olsen

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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.

Original language	English
Journal	Molecular and Cellular Proteomics
Volume	18
Issue number	5
Pages (from-to)	1027-1035
ISSN	1535-9476
DOIs	https://doi.org/10.1074/mcp.TIR118.001270
Publication status	Published - May 2019

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10.1074/mcp.TIR118.001270Licence: CC BY

Protein Aggregation Capture on Microparticles Enables Multipurpose Proteomics Sample PreparationFinal published version, 7.86 MBLicence: CC BY

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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.",

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AU - Batth, Tanveer Singh

AU - Tollenaere, Maxim A. X.

AU - Rüther, Patrick Leopold

AU - Gonzalez-Franquesa, Alba

AU - Prabhakar, Bhargav Saligram

AU - Bekker-Jensen, Simon Holst

AU - Deshmukh, Atul Shahaji

AU - Olsen, Jesper V.

PY - 2019/5

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N2 - 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.

AB - 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.

U2 - 10.1074/mcp.TIR118.001270

DO - 10.1074/mcp.TIR118.001270

M3 - Journal article

C2 - 30833379

SN - 1535-9476

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SP - 1027

EP - 1035

JO - Molecular and Cellular Proteomics

JF - Molecular and Cellular Proteomics

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ER -

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

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