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Single-Molecule Peptide Fingerprinting

By Jetty van Ginkel, Mike Filius, Malwina Szczepaniak, Pawel Tulinski, Anne S. Meyer, Chirlmin Joo

Posted 29 Nov 2017
bioRxiv DOI: 10.1101/226712 (published DOI: 10.1073/pnas.1707207115)

Proteomic analyses provide essential information on molecular pathways of cellular systems and the state of a living organism. Mass spectrometry is currently the first choice for proteomic analysis. However, the requirement for a large amount of sample renders a small-scale proteomics study, such as single-cell analysis, challenging. Here we demonstrate a proof of concept of single-molecule FRET-based protein fingerprinting. We harnessed the AAA+ protease ClpXP to scan peptides. By using donor fluorophore-labeled ClpP, we sequentially read out FRET signals from acceptor-labeled amino acids of peptides. The repurposed ClpXP exhibits uni-directional processing with high processivity and has the potential to detect low-abundance proteins. Our technique is a promising approach for sequencing protein substrates using a small amount of sample.

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