Rapid characterization of secreted recombinant proteins by native mass spectrometry.

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ID: 80221
2018
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Abstract
Characterization of overexpressed proteins is essential for assessing their quality, and providing input for iterative redesign and optimization. This process is typically carried out following purification procedures that require pronounced cost of time and labor. Therefore, quality assessment of recombinant proteins with no prior purification offers a major advantage. Here, we report a native mass spectrometry method that enables characterization of overproduced proteins directly from culture media. Properties such as solubility, molecular weight, folding, assembly state, overall structure, post-translational modifications and binding to relevant biomolecules are immediately revealed. We show the applicability of the method for in-depth characterization of secreted recombinant proteins from eukaryotic systems such as yeast, insect, and human cells. This method, which can be readily extended to high-throughput analysis, considerably shortens the time gap between protein production and characterization, and is particularly suitable for characterizing engineered and mutated proteins, and optimizing yield and quality of overexpressed proteins.
Reference Key
bennissan2018rapidcommunications Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Ben-Nissan, Gili;Vimer, Shay;Warszawski, Shira;Katz, Aliza;Yona, Meital;Unger, Tamar;Peleg, Yoav;Morgenstern, David;Cohen-Dvashi, Hadas;Diskin, Ron;Fleishman, Sarel J;Sharon, Michal;
Journal Communications biology
Year 2018
DOI
10.1038/s42003-018-0231-3
URL
Keywords
personal data general data protection regulation health clinics health data regulation (eu) 2016/679

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