Title: nES GEMMA analysis of lectins and their interactions with glycoproteins – separation, detection, and sampling of noncovalent biospecific complexes
Language: English
Authors: Engel, Nicole Yvonne 
Weiss, Victor
Marchetti-Deschmann, Martina 
Allmaier, Günter
Category: Research Article
Keywords: Lectin; Glycoproteinn; ES GEMMA; CE-on-a-chip; Electrophoresis
Issue Date: 2017
Journal: Journal of The American Society for Mass Spectrometry
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.
DOI: 10.1007/s13361-016-1483-0
Library ID: AC11360826
URN: urn:nbn:at:at-ubtuw:3-2604
ISSN: 1879-1123
Organisation: E164 - Institut für Chemische Technologien und Analytik 
Publication Type: Article
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