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Protease-resistant streptavidin for interaction proteomics

Abstract Streptavidin-mediated enrichment is a powerful strategy to identify biotinylated biomolecules and their interaction partners; however, intense streptavidin-derived peptides impede protein identification by mass spectrometry. Here, we present an approach to chemically modify streptavidin, th...

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Main Authors: Rafiee, Mahmoud-Reza (Author) , Sigismondo, Gianluca (Author) , Kalxdorf, Mathias (Author) , Förster, Laura-Christin (Author) , Brügger, Britta (Author) , Béthune, Julien (Author) , Krijgsveld, Jeroen (Author)
Format: Article (Journal)
Language:English
Published: June 2020
In: Molecular systems biology
Year: 2020, Volume: 16, Issue: 5
ISSN:1744-4292
DOI:10.15252/msb.20199370
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.15252/msb.20199370
Verlag, lizenzpflichtig, Volltext: https://www.embopress.org/doi/full/10.15252/msb.20199370
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Author Notes:Mahmoud-Reza Rafiee, Gianluca Sigismondo, Mathias Kalxdorf, Laura Förster, Britta Brügger, Julien Béthune, & Jeroen Krijgsveld
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Summary:Abstract Streptavidin-mediated enrichment is a powerful strategy to identify biotinylated biomolecules and their interaction partners; however, intense streptavidin-derived peptides impede protein identification by mass spectrometry. Here, we present an approach to chemically modify streptavidin, thus rendering it resistant to proteolysis by trypsin and LysC. This modification results in over 100-fold reduction of streptavidin contamination and in better coverage of proteins interacting with various biotinylated bait molecules (DNA, protein, and lipid) in an overall simplified workflow.
Item Description:Gesehen am 17.8.2020
Physical Description:Online Resource
ISSN:1744-4292
DOI:10.15252/msb.20199370

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