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

31 Citationer (Scopus)

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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.

Originalsprog	Engelsk
Tidsskrift	Molecular and Cellular Proteomics
Vol/bind	18
Udgave nummer	5
Sider (fra-til)	1027-1035
ISSN	1535-9476
DOI	https://doi.org/10.1074/mcp.TIR118.001270
Status	Udgivet - maj 2019

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10.1074/mcp.TIR118.001270Licens: CC BY

Protein Aggregation Capture on Microparticles Enables Multipurpose Proteomics Sample PreparationForlagets udgivne version, 7,86 MBLicens: CC BY

Citationsformater

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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

Abstract

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