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Submicrometer plate heights for capillaries packed with silica colloidal crystals.

ABSTRACT: Extremely uniform packing of colloidal silica in capillaries is shown. Reversed-phase electrochromatograms of DiI-C(12) exhibit plate heights as low as 0.23 microm and a reduced plate height as low as 0.7, using 75 microm i.d. capillaries packed with 330 nm silica particles. The contribution from the A term is 0 +/- 20 nm in electrochromatography. The particles are shown to form colloidal crystals inside the capillaries. Optical images show Bragg diffraction, indicative of crystallinity. Scanning electron microscopy (SEM) images show face-centered cubic crystallinity, and the porosity is 0.25 +/- 0.01, which is in agreement with that for face-centered cubic crystals. The capillaries are fritless, and 100 microm i.d. capillaries packed with silica colloidal crystals withstand pressures of at least 12,400 psi.

SUBMITTER: Malkin DS

PROVIDER: S-EPMC3018733 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature

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Submicrometer plate heights for capillaries packed with silica colloidal crystals.

Malkin Douglas S DS Wei Bingchuan B Fogiel Arthur J AJ Staats Sau Lan SL Wirth Mary J MJ

Analytical chemistry 20100301 6

Extremely uniform packing of colloidal silica in capillaries is shown. Reversed-phase electrochromatograms of DiI-C(12) exhibit plate heights as low as 0.23 microm and a reduced plate height as low as 0.7, using 75 microm i.d. capillaries packed with 330 nm silica particles. The contribution from the A term is 0 +/- 20 nm in electrochromatography. The particles are shown to form colloidal crystals inside the capillaries. Optical images show Bragg diffraction, indicative of crystallinity. Scannin ...[more]

PMID: 20158216

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Project description:The use of submicrometer capillaries for nanoelectrospray ionization of native proteins and protein complexes effectively reduces the number of nonspecific salt adducts to biological molecules, therefore increasing the apparent resolution of a mass spectrometer without any further instrument modifications or increased ion activation. However, the increased interaction between proteins and the surface of the capillary has been shown to promote protein expansion and therefore loss of native structure. Here, we compare the effect of micrometer and submicrometer sized capillaries on the native structures of the protein complexes streptavidin, concanavalin A, and C-reactive protein under charge reducing conditions. We observe that the use of submicrometer capillaries did not result in a significantly higher charge state distribution, indicative of expansion, when compared to micrometer sized capillaries for complexes in 100 mM ammonium acetate and 100 mM triethylammonium acetate and for streptavidin in 200 mM ammonium acetate with no charge reduction. Additionally, no significant differences in collision cross sections were observed using ion mobility mass spectrometry. Finally, the dissociation behaviors of protein complexes ionized using micrometer and submicrometer capillaries were compared to determine if any structural perturbation occurred during ionization. Protein complexes from both capillary sizes displayed similar surface-induced dissociation patterns at similar activation energies. The results suggest that submicrometer capillaries do not result in significant changes to protein complex structure under charge reducing conditions and may be used for native mass spectrometry experiments. Submicrometer capillaries can be used to resolve small mass differences of biological systems on a QTOF platform; however, a laser tip puller is required for pulling reproducible submicrometer capillaries, and disruption in spray due to clogging was observed for larger protein complexes.

Dataset Information

Submicrometer plate heights for capillaries packed with silica colloidal crystals.

Publications

Submicrometer plate heights for capillaries packed with silica colloidal crystals.

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