Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum

Timothy N. Tiambeng; David S. Roberts; Kyle A. Brown; Yanlong Zhu; Bifan Chen; Zhijie Wu; Stanford D. Mitchell; Tania M. Guardado-Alvarez; Song Jin; Ying Ge

doi:10.1038/s41467-020-17643-1

Nature Communications (Aug 2020)

Nanoproteomics enables proteoform-resolved analysis of low-abundance proteins in human serum

Timothy N. Tiambeng,
David S. Roberts,
Kyle A. Brown,
Yanlong Zhu,
Bifan Chen,
Zhijie Wu,
Stanford D. Mitchell,
Tania M. Guardado-Alvarez,
Song Jin,
Ying Ge

Affiliations

Timothy N. Tiambeng: Department of Chemistry, University of Wisconsin—Madison
David S. Roberts: Department of Chemistry, University of Wisconsin—Madison
Kyle A. Brown: Department of Chemistry, University of Wisconsin—Madison
Yanlong Zhu: Human Proteomics Program, School of Medicine and Public Health, University of Wisconsin—Madison
Bifan Chen: Department of Chemistry, University of Wisconsin—Madison
Zhijie Wu: Department of Chemistry, University of Wisconsin—Madison
Stanford D. Mitchell: Department of Cell and Regenerative Biology, University of Wisconsin—Madison
Tania M. Guardado-Alvarez: Department of Chemistry, University of Wisconsin—Madison
Song Jin: Department of Chemistry, University of Wisconsin—Madison
Ying Ge: Department of Chemistry, University of Wisconsin—Madison

DOI: https://doi.org/10.1038/s41467-020-17643-1
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 12

Abstract

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Top-down proteomics can provide unique insights into the biological variations of protein biomarkers but detecting low-abundance proteins in body fluids remains challenging. Here, the authors develop a nanoparticle-based top-down proteomics approach enabling enrichment and detailed analysis of cardiac troponin I in human serum.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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