Hydrophobic Interaction Chromatography of Proteins, Nucleic Acids, Viruses, and Cells on Noncharged Amphiphilic Gels

Hjertén, Stellan

doi:10.1002/9780470110478.ch2

Cited by 50 publications

(2 citation statements)

References 58 publications

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“…To measure the relative hydrophobicity of the organic coatings alone, precipitation experiments were performed by adding ammonium sulfate to sodium citrate, GA, and PVP following Andrews et al Briefly, sodium citrate, GA, or PVP was added to 50 mL of sodium phosphate buffer (0.05 M, pH 8), as specified in the method used for determining the relative hydrophobicity of macromolecules and proteins . Solid ammonium sulfate was added into the polymer or citrate solutions until the material precipitated (i.e., the cloud point).…”

Section: Methodsmentioning

confidence: 99%

Hydrophobic Interactions Increase Attachment of Gum Arabic- and PVP-Coated Ag Nanoparticles to Hydrophobic Surfaces

Song

Phenrat

Marinakos

et al. 2011

Environ. Sci. Technol.

138

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A fundamental understanding of attachment of surface-coated nanoparticles (NPs) is essential to predict the distribution and potential risks of NPs in the environment. Column deposition studies were used to examine the effect of surface-coating hydrophobicity on NP attachment to collector surfaces in mixtures with varying ratios of octadecylichlorosilane (OTS)-coated (hydrophobic) glass beads and clean silica (hydrophilic) glass beads. Silver nanoparticles (AgNPs) coated with organic coatings of varying hydrophobicity, including citrate, polyvinylpyrrolidone (PVP), and gum arabic (GA), were used. The attachment efficiencies of GA and PVP AgNPs increased by 2- and 4-fold, respectively, for OTS-coated glass beads compared to clean glass beads. Citrate AgNPs showed no substantial change in attachment efficiency for hydrophobic compared to hydrophilic surfaces. The attachment efficiency of PVP-, GA-, and citrate-coated AgNPs to hydrophobic collector surfaces correlated with the relative hydrophobicity of the coatings. The differences in the observed attachment efficiencies among AgNPs could not be explained by classical DLVO, suggesting that hydrophobic interactions between AgNPs and OTS-coated glass beads were responsible for the increase in attachment of surface-coated AgNPs with greater hydrophobicity. This study indicates that the overall attachment efficiency of AgNPs will be influenced by the hydrophobicity of the NP coating and the fraction of hydrophobic surfaces in the environment.

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Section: Methodsmentioning

confidence: 99%

Hydrophobic Interactions Increase Attachment of Gum Arabic- and PVP-Coated Ag Nanoparticles to Hydrophobic Surfaces

Song

Phenrat

Marinakos

et al. 2011

Environ. Sci. Technol.

138

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show abstract

“…This can be achieved using various chromatographic methods, including ion exchange [46], reversed phase [47], hydrophobic interaction [48], size exclusion or the more popular SDS polyacrylamide gel electrophoresis (SDS PAGE) separation [42]. Alternatively, peptide can be fractionated using several methods like OFFGEL fractionation [49], high pH fractionation [33], strong cation exchange chromatography [50] or strong anion exchange chromatography [51].…”

Section: Emerging Technology For Skeletal Muscle Proteomementioning

confidence: 99%

Proteomics of Skeletal Muscle: Focus on Insulin Resistance and Exercise Biology

Deshmukh

2016

Proteomes

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Skeletal muscle is the largest tissue in the human body and plays an important role in locomotion and whole body metabolism. It accounts for ~80% of insulin stimulated glucose disposal. Skeletal muscle insulin resistance, a primary feature of Type 2 diabetes, is caused by a decreased ability of muscle to respond to circulating insulin. Physical exercise improves insulin sensitivity and whole body metabolism and remains one of the most promising interventions for the prevention of Type 2 diabetes. Insulin resistance and exercise adaptations in skeletal muscle might be a cause, or consequence, of altered protein expressions profiles and/or their posttranslational modifications (PTMs). Mass spectrometry (MS)-based proteomics offer enormous promise for investigating the molecular mechanisms underlying skeletal muscle insulin resistance and exercise-induced adaptation; however, skeletal muscle proteomics are challenging. This review describes the technical limitations of skeletal muscle proteomics as well as emerging developments in proteomics workflow with respect to samples preparation, liquid chromatography (LC), MS and computational analysis. These technologies have not yet been fully exploited in the field of skeletal muscle proteomics. Future studies that involve state-of-the-art proteomics technology will broaden our understanding of exercise-induced adaptations as well as molecular pathogenesis of insulin resistance. This could lead to the identification of new therapeutic targets.

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Chromatography, Hydrophobic Interaction

Kårsnäs¹

1999

Encyclopedia of Bioprocess Technology

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Hydrophobic Interaction Chromatography of Proteins, Nucleic Acids, Viruses, and Cells on Noncharged Amphiphilic Gels

Cited by 50 publications

References 58 publications

Hydrophobic Interactions Increase Attachment of Gum Arabic- and PVP-Coated Ag Nanoparticles to Hydrophobic Surfaces

Hydrophobic Interactions Increase Attachment of Gum Arabic- and PVP-Coated Ag Nanoparticles to Hydrophobic Surfaces

Proteomics of Skeletal Muscle: Focus on Insulin Resistance and Exercise Biology

Chromatography, Hydrophobic Interaction

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