ArticleACS chemical biology2020
Solid-Phase Peptide Capture and Release for Bulk and Single-Molecule Proteomics.
Article in ACS chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Unlocking the Silent Proteome: Chemoselective Asn/Gln Activation for Multidimensional Protein Diversification.Journal of the American Chemical Society · 2026Article
- Reversible Conjugation of Polypeptides and Proteins Utilizing a [3.3.1] Scaffold under Mild Conditions.Organic letters · 2024Article
- A Method for Rigorously Selective Capture and Simultaneous Fluorescent Labeling of N-Terminal Glycine Peptides.Journal of the American Chemical Society · 2024Article
- Single-molecule fluorescence methods for protein biomarker analysis.Analytical and bioanalytical chemistry · 2023Review
- Protein Sequencing, One Molecule at a Time.Annual review of biophysics · 2022Review
- Cataloguing the proteome: Current developments in single-molecule protein sequencing.Biophysics reviews · 2022Review
- Photoredox-Catalyzed DecarboxylativeACS chemical biology · 2021Article
- Herding cats: Label-based approaches in protein translocation through nanopore sensors for single-molecule protein sequence analysis.iScience · 2021Review
- The emerging landscape of single-molecule protein sequencing technologies.Nature methods · 2021Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The field of proteomics has expanded recently with more sensitive techniques for the bulk measurement of peptides as well as single-molecule techniques. One limiting factor for some of these methods is the need for multiple chemical derivatizations and highly pure proteins free of contaminants. We demonstrate a solid-phase capture-release strategy suitable for the proteolysis, purification, and subsequent chemical modification of peptides. We use this resin on an HEK293T cell lysate and perform one-pot proteolysis, capture, and derivatization to survey peptide capture biases from over 40 000 unique peptides from a cellular proteome. We also show that this capture can be reversed in a traceless manner, such that it is amenable for single-molecule proteomics techniques. With this technique, we perform a fluorescent labeling and C-terminal derivatization on a peptide and subject it to fluorosequencing, demonstrating that washing the resin is sufficient to remove excess dyes and other reagents prior to single-molecule protein sequencing.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.