Analysis of biomolecules using electrospray and nanoparticle methods

Kaufman, Stanley L.

doi:10.1016/s0021-8502(97)00462-x

Cited by 83 publications

(64 citation statements)

References 55 publications

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“…Charge reduction of the sprayed droplets to unity is essential for the sizing method. 15 In an electrical-mobility detection technique (DMA), the aerosol passes through a bipolar ion neutralizer, which generates a high level of positive and negative ions. The neutralizer brings the aerosol charge level to a Fuch's equilibrium charge distribution.…”

Section: Methodsmentioning

confidence: 99%

Sizing of Colloidal Nanoparticles by Electrospray and Differential Mobility Analyzer Methods

et al. 2002

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The goal of this work was to develop a simple technique for sizing colloidal particles by means of electrospray and aerosol techniques. Size distribution of different types of colloids (oxides, metals, and polymers) such as silica, gold, palladium, and polystyrene latex particles, with different nominal sizes below 100 nm was determined online. Nanometer-sized particles were dispersed into the gas phase as an aerosol via electrosprays operating in the cone-jet mode of a colloidal solution followed by a charge reduction of the sprayed droplets to unity and subsequent evaporation of the solvent. The size distribution of the generated aerosol particles was then determined by a differential mobility analyzer combined with a condensation nucleus/particle counter. For comparison, particle sizes were determined by electron microscopy (EM) using the samples which were obtained by (i) naturally dried sols and (ii) on-line deposited on a substrate during electrospraying. The proposed technique is capable of detecting the degree of dispersity of all colloid samples, and the measured values were comparable to results obtained by EM and dynamic light scattering. The results clearly show that the method described here constitutes a convenient, reliable, and rapid tool for the size determination of colloidal nanoparticles.

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Section: Methodsmentioning

confidence: 99%

Sizing of Colloidal Nanoparticles by Electrospray and Differential Mobility Analyzer Methods

et al. 2002

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“…interrogation of whole proteins on proteome scale in the gas-phase, also demand accurate mass calibration of mass spectrometer at high m/z values. In addition to the examples discussed above, alternative approaches such as nanoelectromechanical mass spectrometry [110], on a gas-phase electrophoretic mobility molecular analyzer (GEMMA) [111] have been used to record the mass of particles up to 100 MDa (for a recent review see [112]). …”

Section: Mass Calibration At High Mass-to-charge Ratiosmentioning

confidence: 99%

Mass spectrometric methods to analyze the structural organization of macromolecular complexes

Rajabi

Ashcroft

Radford

2015

Methods

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With the development of soft ionization techniques such as electrospray ionization (ESI), mass spectrometry (MS) has found widespread application in structural biology. The ability to transfer large biomolecular complexes intact into the gas-phase, combined with the low sample consumption and high sensitivity of MS, has made ESI-MS a method of choice for the characterization of macromolecules. This paper describes the application of MS to study large non-covalent complexes. We categorize the available techniques in two groups. First, solution-based techniques in which the biomolecules are labeled in solution and subsequently characterized by MS. Three MS-based techniques are discussed, namely hydroxyl radical footprinting, cross-linking and hydrogen/deuterium exchange (HDX) MS. In the second group, MS-based techniques to probe intact biomolecules in the gas-phase, e.g. side-chain microsolvation, HDX and ion mobility spectrometry are discussed. Together, the approaches place MS as a powerful methodology for an ever growing plethora of structural applications.

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“…As previously described by Kaufman in detail [3], nES GEMMA separates analytes according to their electrophoretic mobility diameter (EMD) in the gas phase, which can directly be correlated to the dry particle diameters in the nm range. Consequently, the molecular weights can be calculated by application of a correlation derived from respective standard compounds [3, 4].…”

Section: Introductionmentioning

confidence: 99%

“…Consequently, the molecular weights can be calculated by application of a correlation derived from respective standard compounds [3, 4]. In brief, multiply charged droplets produced in cone jet mode in the nES unit are dried and simultaneously charge-reduced in a bipolar atmosphere (induced by a 210 Po source) and subsequently introduced into the nano differential mobility analyzer (nDMA).…”

Section: Introductionmentioning

confidence: 99%

nES GEMMA Analysis of Lectins and Their Interactions with Glycoproteins – Separation, Detection, and Sampling of Noncovalent Biospecific Complexes

Engel

Weiss

Marchetti‐Deschmann

et al. 2016

J. Am. Soc. Mass Spectrom.

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In order to better understand biological events, lectin–glycoprotein interactions are of interest. The possibility to gather more information than the mere positive or negative response for interactions brought mass spectrometry into the center of many research fields. The presented work shows the potential of a nano-electrospray gas-phase electrophoretic mobility molecular analyzer (nES GEMMA) to detect weak, noncovalent, biospecific interactions besides still unbound glycoproteins and unreacted lectins without prior liquid phase separation. First results for Sambucus nigra agglutinin, concanavalin A, and wheat germ agglutinin and their retained noncovalent interactions with glycoproteins in the gas phase are presented. Electrophoretic mobility diameters (EMDs) were obtained by nES GEMMA for all interaction partners correlating very well with molecular masses determined by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) of the individual molecules. Moreover, EMDs measured for the lectin–glycoprotein complexes were in good accordance with theoretically calculated mass values. Special focus was laid on complex formation for different lectin concentrations and binding specificities to evaluate the method with respect to results obtained in the liquid phase. The latter was addressed by capillary electrophoresis on-a-chip (CE-on-a-chip). Of exceptional interest was the fact that the formed complexes could be sampled according to their size onto nitrocellulose membranes after gas-phase separation. Subsequent immunological investigation further proved that the collected complex actually retained its native structure throughout nES GEMMA analysis and sampling. Graphical Abstractᅟ Electronic supplementary materialThe online version of this article (doi:10.1007/s13361-016-1483-0) contains supplementary material, which is available to authorized users.

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Analysis of biomolecules using electrospray and nanoparticle methods

Cited by 83 publications

References 55 publications

Sizing of Colloidal Nanoparticles by Electrospray and Differential Mobility Analyzer Methods

Sizing of Colloidal Nanoparticles by Electrospray and Differential Mobility Analyzer Methods

Mass spectrometric methods to analyze the structural organization of macromolecular complexes

nES GEMMA Analysis of Lectins and Their Interactions with Glycoproteins – Separation, Detection, and Sampling of Noncovalent Biospecific Complexes

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