Perfluorooctanoic acid and ammonium perfluorooctanoate: volatile surfactants for proteome analysis?

Vieira, Douglas B.; Crowell, Andrew M.J.; Doucette, Alan A.

doi:10.1002/rcm.6127

Cited by 13 publications

(15 citation statements)

References 36 publications

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“…To address the poor MS compatibility of detergents like SDS, where an upper limit threshold for the presence of SDS in sample is only 0.01% , several new acid‐labile detergents have been commercialized within the past decade. These include sodium 3‐[(2‐methyl‐2‐undecyl‐1,3‐dioxolan‐4‐yl)methoxy]‐1‐propanesulfonate (RapiGest, Waters) and 3‐[3‐(1,1‐bisalkyloxyethyl)pyridin‐1‐yl]propane‐1‐sulfonate (PPS, Protein Discovery).…”

Section: Solubilization Of Mps and Ms Compatibilitymentioning

confidence: 99%

“…However, the data indicated significant improvements in hydrophobic peptide recovery, especially for late‐eluting peptides, with even ten‐fold enhancements in intensity for some peptides reported. More recently, there has been interest in the use of fluorinated surfactants as alternatives to SDS, with ammonium perfluorooctanoate (2–4% w/v) found to have good solubilization ability, and easy removal by evaporation after acidification .…”

Section: Solubilization Of Mps and Ms Compatibilitymentioning

confidence: 99%

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Membrane proteomics by high performance liquid chromatography–tandem mass spectrometry: Analytical approaches and challenges

et al. 2013

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Membrane proteins (MPs) play diverse biologically important structural and functional roles including molecular transport, cell communication, and signal transduction. The dysfunctions of many are linked to deleterious human diseases and thus are of utmost importance in drug discovery. MPs comprise approximately 20–30% of all open reading frames (ORFs), however they are typically under‐represented in many LC‐MS proteomics experiments due to their low abundance and poor solubility. To address these analytical challenges, various MP enrichment, solubilization, digestion, and fractionation strategies have been employed to further improve the coverage of the membrane systems while maintaining compatibility with MS detection. This review discusses both established and emerging high‐throughput gel‐free analytical workflows in membrane proteomics, and the inherent advantages, disadvantages, and orthogonality of the various approaches. The issues of critical importance for successful LC‐MS/MS detection such as detergent selection and minimizing ion suppression in detergent‐based workflows are discussed in detail. Recent studies comparing the performance of different analytical strategies are highlighted in order to provide practical insight into the choice of the most appropriate method for membrane‐centric applications ranging from cell surface biomarker discovery to MP interaction network mapping.

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Section: Solubilization Of Mps and Ms Compatibilitymentioning

confidence: 99%

Section: Solubilization Of Mps and Ms Compatibilitymentioning

confidence: 99%

Membrane proteomics by high performance liquid chromatography–tandem mass spectrometry: Analytical approaches and challenges

et al. 2013

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“…Surfactants are used in proteomic research to facilitate solubilization and digestion of proteins . We and others recently reported that a volatile surfactant, perfluorooctanoic acid (PFOA), solubilizes membrane proteins as effectively as sodium dodecyl sulfate (SDS) , the gold standard in protein solubilization. Unlike SDS, PFOA (up to 0.5%, w/v) does not inhibit trypsin activity, making the surfactant compatible with protein digestion by trypsin .…”

Section: Recoveries Of Bsa Peptides From Scx Hilic and Fspementioning

confidence: 99%

“…The evaporation of PFOA is achieved by repeatedly evaporating and reconstituting the protein digests from ethanol:ethylacetate:water:TFA (0.33:0.33:0.33:0.01, v/v/v/v) under both in vacuo and atmospheric pressure . The evaporation procedure is a lengthy process taking approximately 6 h. Although, Vieira and co‐workers have recently reported that PFOA can be evaporated from 50 mM HCl in 2 h , finding a more rapid alternative would increase the relevance of PFOA in proteomic research.…”

Section: Recoveries Of Bsa Peptides From Scx Hilic and Fspementioning

confidence: 99%

Rapid and effective removal of perfluorooctanoic acid from proteomics samples

et al. 2012

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We recently demonstrated that perfluorooctanoic acid (PFOA), a volatile surfactant, is as effective as sodium dodecyl sulfate (SDS) at solubilizing membrane proteins. PFOA can be removed by repeated evaporation prior to mass spectrometry analysis. However, removal of PFOA by evaporation is a lengthy process that takes approximately 6 hrs. Toward the goal of decreasing the length of time required to remove PFOA from protein digests, we tested the efficiency of PFOA removal and subsequent peptide recovery using strong cation exchange (SCX) chromatography, hydrophilic interaction chromatography (HILIC), fluorous solid phase extraction (FSPE), and anion exchange chromatography (ANX). We found that all these chromatographic techniques except ANX chromatography remove PFOA thoroughly from protein digest. Peptide recovery rates from SCX chromatography varied widely; non-acidic peptides were recovered at rates of up to 95%, and acidic peptides were recovered at rates of less than 10%. On the other hand, acidic peptides were recovered well from HILIC, while peptides whose pIs are greater than 6 were recovered poorly. Peptide recovery using FSPE was considerably lower, less than 10% for most of the peptides. These results indicate that SCX and HILIC chromatography provide a more rapid alternative to the evaporation method for applications in which recovery of entire set of peptides is not required.

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“…Isomeric ions are separated by IMS-MS while migrating through a buffer gas with a drift velocity that will depend on the charge, shape (collision cross-section, CCS) and polarity. 17 IMS has been mainly used to analyze compounds such as drugs, chemical warfare agents, explosives, environmental pollutants, dendrimeric and polymeric structures, as well as proteins and peptides, 18,19 providing invaluable information about their conformation in the native solution environment. 20 Traveling wave ion mobility (TWIM) has been introduced more recently as a new mode of ion propulsion for IMS experiments.…”

Section: Introductionmentioning

confidence: 99%

Corrole isomers: intrinsic gas-phase shapes via traveling wave ion mobility mass spectrometry and dissociation chemistries via tandem mass spectrometry

et al. 2012

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PAPERCorrole and four of its isomers with subtle structural changes promoted by exchange of nitrogen and carbon atoms in the corrole ring have been studied by traveling wave ion mobility mass spectrometry and collision induced dissociation experiments. Significant differences in shapes and charge distributions for their protonated molecules were found to lead to contrasting gas phase mobilities, most particularly for corrorin, the most "confused" isomer. Accordingly, corrorin was predicted by B3LYP/6-31g(d,p) and collisional cross section calculations to display the most compact tri-dimensional structure, whereas NCC4 and corrole were found to be the most planar isomers. Better resolution between the corrole isomers was achieved using the more polarizable and massive CO 2 as the drift gas. Sequential losses of HF molecules were found to dominate the dissociation chemistry of the protonated molecules of these corrole isomers, but their unique structures caused contrasting labilities towards CID, whereas NCC4 showed a peculiar and structurally diagnostic loss of NH 3 , allowing its prompt differentiation from the other isomers.

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Perfluorooctanoic acid and ammonium perfluorooctanoate: volatile surfactants for proteome analysis?

Cited by 13 publications

References 36 publications

Membrane proteomics by high performance liquid chromatography–tandem mass spectrometry: Analytical approaches and challenges

Membrane proteomics by high performance liquid chromatography–tandem mass spectrometry: Analytical approaches and challenges

Rapid and effective removal of perfluorooctanoic acid from proteomics samples

Corrole isomers: intrinsic gas-phase shapes via traveling wave ion mobility mass spectrometry and dissociation chemistries via tandem mass spectrometry

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