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John E Schiel

John's primary research focus at NIST involves physicochemical characterization of biopharmaceuticals and other glycoproteins. Biopharmaceuticals are highly complex, heterogeneous glycoproteins that represent the most rapidly growing class of therapeutic. A variety of analytical assays are required to establish product identity, understand degradation pathways, and validate comparability exercises to ensure process reproducibility or biosimilarity. John develops and utilizes mass spectrometry-based protocols for analysis of primary sequence, glycoprofile, and other post-translational modifications. Candidate test methods are explored to identify critical biopharmaceutical test metrics. This technology is currently being applied to the development of an IgG reference material useful for biopharmaceutical characterization throughout the drug product lifecycle.

John also conducts basic glycoanalytical research to increase the variety of methodology for glycosylation site determination, glycan identity, and glycoform quantification. Current research revolves around the improvement of glycoanalytical traceability and reproducibility through quantitative measurements.


Awards


  • Featured "Young Investigator in Analytical and Bioanalytical Science", 2012 (ABC, 403, 2279-2289)
  • NIST Sigma Xi Most Outstanding Poster Award, 2010 and 2011
  • Sigma Xi Outstanding Graduate Award, 2009
  • Bioanalysis Young Investigator Award, 2009 (Bioanalysis, 1, 17-18)
  • American Chemical Society Division of Analytical Chemistry Fellowship, 2007 (Anal. Chem., 79, 385)


Membership and Professional Activities


American Society for Mass Spectrometry


Selected Publications:

Schiel, J. E. Glycoprotein analysis using mass spectrometry: unraveling the layers of complexity. Analytical and Bioanalytical Chemistry 2012, 404 (4), 1141-1149.

Schiel, J. E.; Au, J.; He, H. J.; Phinney, K. W. LC-MS/MS biopharmaceutical glycoanalysis: identification of desirable reference material characteristics. Analytical and Bioanalytical Chemistry 2012, 403 (8), 2279-2289.

Schiel, J. E.; Lowenthal, M. S.; Phinney, K. W. Mass spectrometry characterization for chemoenzymatic glycoprotein synthesis. Journal of Mass Spectrometry 2011, 46 (7), 649-657.

Lowenthal, M. S.; Gasca-Aragon, H.; Schiel, J. E.; Dodder, N. G.; Bunk, D. M. A quantitative LC-MS/MS method for comparative analysis of capture-antibody affinity toward protein antigens. Journal of Chromatography B-Analytical Technologies in the Biomedical and Life Sciences 2011, 879 (26), 2726-2732.

Schiel, J. E.; Tong, Z. H.; Sakulthaew, C.; Hage, D. S. Development of a Flow-Based Ultrafast Immunoextraction and Reverse Displacement Immunoassay: Analysis of Free Drug Fractions. Analytical Chemistry 2011, 83 (24), 9384-9390.

Tong, Z. H.; Schiel, J. E.; Papastavros, E.; Ohnmacht, C. M.; Smith, Q. R.; Hage, D. S. Kinetic studies of drug-protein interactions by using peak profiling and high-performance affinity chromatography: Examination of multi-site interactions of drugs with human serum albumin columns. Journal of Chromatography A 2011, 1218 (15), 2065-2071.

Yoo, M. J.; Schiel, J. E.; Hage, D. S. Evaluation of affinity microcolumns containing human serum albumin for rapid analysis of drug-protein binding. Journal of Chromatography B-Analytical Technologies in the Biomedical and Life Sciences 2010, 878 (20), 1707-1713.

Schiel, J. E.; Joseph, K. S.; Hage, D. S. Biointeraction Affinity Chromatography: General Principles and Recent Developments. Advances in Chromatography, Vol 48 2010, 48, 145-193.

Schiel, J. E.; Hage, D. S. Kinetic studies of biological interactions by affinity chromatography. Journal of Separation Science 2009, 32 (10), 1507-1522.

Schiel, J. E.; Ohnmacht, C. M.; Hage, D. S. Measurement of Drug-Protein Dissociation Rates by High-Performance Affinity Chromatography and Peak Profiling. Analytical Chemistry 2009, 81 (11), 4320-4333.

Schiel, J. E.; Mallik, R.; Soman, S.; Joseph, K. S.; Hage, D. S. Applications of silica supports in affinity chromatography. Journal of Separation Science 2006, 29 (6), 719-737.

Publications

Glycan Analysis of NIST mAb Reference Material

Author(s)
John E. Schiel, Catherine A. Mouchahoir
N-linked glycosylation is a common post-translational modification that imparts structural heterogeneity to recombinant monoclonal antibody therapeutics. The

Determination of the Primary Sequence/ Structure

Author(s)
Catherine A. Mouchahoir, Mellisa Ly, Michaella Levy, Lisa E. Kilpatrick, Scott C. Lute, Karen W. Phinney, Lisa Marzilli, Kurt A. Brorson, Michael T. Boyne, Darryl Davis, John E. Schiel
The primary sequence of a protein, including therapeutic monoclonal antibodies (mAbs), is a critical quality attribute that determines a great deal of its
Created September 24, 2019