ArticleThe Journal of membrane biology2014
APols-aided protein precipitation: a rapid method for concentrating proteins for proteomic analysis.
Article in The Journal of membrane biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- Advances in Crystallography and Cryo-Electron Microscopy for the Study of Membrane Proteins.Advances in experimental medicine and biology · 2026Review
- Human mesenchymal stem cell secretomes: Factors affecting profiling and challenges in clinical application.Cell and tissue research · 2024Review
- A Strong Cation Exchange Chromatography Protocol for Examining N-Terminal Proteoforms.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Small Protein Enrichment Improves Proteomics Detection of sORF Encoded Polypeptides.Frontiers in genetics · 2021Article
- CapturingFrontiers in medicine · 2021Article
- Analyzing trapped protein complexes by Virotrap and SFINX.Nature protocols · 2017Article
- Amphipols for each season.The Journal of membrane biology · 2014Review
- ATP13A3 is a major component of the enigmatic mammalian polyamine transport system.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Amphipols (APols) are a newly designed and milder class of detergent. They have been used primarily in protein structure analysis for membrane protein trapping and stabilization. We have recently demonstrated that APols can be used as an alternative detergent for proteome extraction and digestion, to achieve a "One-stop" single-tube workflow for proteomics. In this workflow, APols are removed by precipitation after protein digestion without depleting the digested peptides. Here, we took further advantage of this precipitation characteristic of APols to concentrate proteins from diluted samples. In contrast with tryptic peptides, a decrease in pH leads to the unbiased co-precipitation of APols with proteins, including globular hydrophilic proteins. We demonstrated that this precipitation is a combined effect of acid precipitation and the APols' protein interactions. Also, we have been able to demonstrate that APols-aided protein precipitation works well on diluted samples, such as secretome sample, and provides a rapid method for protein concentration.
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Registered trials
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