Philosophy and Neuroscience

Corradini, Antonella

doi:10.1515/9783110325782.203

Cited by 3 publications

(2 citation statements)

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“…Adsorption of the analytes is undesirable in capillary electrophoresis because it results in peak dispersion and peak asymmetry; several mathematical models have been elaborated to quantitate the consequences of this chromatographic effect in capillary electrophoresis [5][6][7][8][9]. The various experimental attempts to prevent protein-wall interactions can be classified into four categories [lo]: (i) use of buffers of extreme pH [4] or high ionic strength [3], and utilization of buffer additives such as zwitterions [ll], amines [12], or surfactants [ 131; (ii) traditional silane coupling chemistry [14-161; (iii) physical adsorption of polymers, e. g. polyvinylal-coho1 [17], polyethyleneimine [18,191, nonionic surfactants [20], cellulose acetate [21] or hexadimethrin bromide [22], onto the capillary surface; and (iv) chemically bonding a polymer to the capillary wall, which is the most frequently applied strategy to eliminate adsorption sites [23]. Some of the more prominent examples of immobilized polymers are polyacrylamide [24-261, polyoxyethylene [27, 281, polyethyleneimine [29], polysaccharides [30], and polyvinylalcohol [3 13.…”

Section: Introductionmentioning

confidence: 99%

Capillary electrophoresis of peptides and proteins in fused‐silica capillaries coated with derivatized polystyrene nanoparticles

Kleindienst

Huber

Gjerde³

et al. 1998

Electrophoresis

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High-resolution capillary electrophoretic separation of proteins and peptides was achieved by coating the inner wall of 75 microm ID fused-silica capillaries with 40-140 nm polystyrene particles which have been derivatized with alpha-omega-diamines such as ethylenediamine or 1,10-diaminodecane. A stable and irreversibly adsorbed coating was obtained upon deprotonation of the capillary surface with aqueous sodium hydroxide and subsequent flushing with a suspension of the positively charged particles. At pH 3.1, the detrimental adsorption of proteins to the capillary inner wall was suppressed efficiently because of electrostatic repulsion of the positively charged proteins from the positively charged coating which enabled protein separations with maximum efficiencies of 400000 plates per meter. A substantial improvement of separation efficiency in particle-coated capillaries was observed after in-column derivatization of amino functionalities with 2,3-epoxy-l-propanol, resulting in a more hydrophilic coating. Five basic and four acidic proteins could be separated in less than 7 min with efficiencies up to 1900000 theoretical plates per meter. Finally, coated capillaries were applied to the high-resolution analysis of protein glycoforms and bioactive peptides.

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Section: Introductionmentioning

confidence: 99%

Capillary electrophoresis of peptides and proteins in fused‐silica capillaries coated with derivatized polystyrene nanoparticles

Kleindienst

Huber

Gjerde³

et al. 1998

Electrophoresis

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“…In the last approach, various types of additives were employed. For example, cationic surfactants [ll-121, primary alkyldiamines [13-141, tertiary alkylamines [14][15][16], bis-quaternary ammonium alkanes [17], amino sugars [15], and chitosan [18]. Most of these additives have been reported to reverse the direction of the electroosmotic flow from cathodic to anodic [ll, 12, 15-18].…”

Section: Introductionmentioning

confidence: 99%

N,N,N′,N′‐Tetramethyl‐1,3‐butanediamine as effective running electrolyte additive for efficient electrophoretic separation of basic proteins in bare fused‐silica capillaries

Corradini

Cannarsa

1995

Electrophoresis

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The effect of N,N,N',N'-tetramethyl-1,3-butanediamine (TMBD) in the running electrolyte on the electroosmotic flow and the migration behavior of four standard basic proteins in bare fused-silica capillaries was examined at pH 4.0, 5.5, and 6.5. Depending on the electrolyte pH and additive concentration the electroosmotic flow was either cathodic or anodic. A similar Langmuirian-type dependence of the electroosmotic flow on the concentration of TMBD in the running electrolyte was found at the three experimented pH values, which may be indicative of the specific adsorption of the additive in the immobilized region of the electric double layer at the interface between the capillary wall and the electrolyte solution. Electrophoretic separations of the four standard basic proteins performed at the three above pH values, showed well-resolved, efficient and symmetric peaks, demonstrating the utility of this additive for protein electrophoresis in bare fused-silica capillaries. The variations in separation efficiency, peak capacity, resolution and reproducibility of migration times as a function of the additive concentration at pH 6.5 were also examined.

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Mirroring mirror neurons in an interdisciplinary debate

Antonietti¹,

Corradini²

2013

Consciousness and Cognition

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Philosophy and Neuroscience

Cited by 3 publications

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Capillary electrophoresis of peptides and proteins in fused‐silica capillaries coated with derivatized polystyrene nanoparticles

Capillary electrophoresis of peptides and proteins in fused‐silica capillaries coated with derivatized polystyrene nanoparticles

N,N,N′,N′‐Tetramethyl‐1,3‐butanediamine as effective running electrolyte additive for efficient electrophoretic separation of basic proteins in bare fused‐silica capillaries

Mirroring mirror neurons in an interdisciplinary debate

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