Cupriavidus necator, an alternative source for isotopic enrichment of proteins expressed in insect cells for NMR investigations

Isotopic enrichment of pharmacologically relevant protein targets is crucial for structural studies by nuclear magnetic resonance (NMR) and plays a key role in advancing structure-guided drug discovery. Many clinically important drug targets require expression in eukaryotic systems-such as mammalian, yeast, or insect cells-rather than prokaryotic hosts. This requirement limits the feasibility of high-throughput isotopic labeling and poses challenges for obtaining uniformly isotope-labeled proteins suitable for NMR analysis. While several enrichment strategies have been developed, no broadly applicable enrichment platform has emerged for eukaryotic expression systems. In this study, we introduce Cupriavidus necator as an alternative biological source for <sup>15</sup>N and <sup>13</sup>C isotopic enrichment to support protein production in eukaryotic systems. To evaluate this approach, we selected the kinase domain of EPHA2, a receptor tyrosine kinase implicated in colorectal cancer progression and an important target for therapeutic inhibitor development. Isotopic incorporation was quantified using liquid chromatography-mass spectrometry (LC-MS), revealing enrichment levels of 79% for <sup>15</sup>N and 69% for <sup>13</sup>C. These results demonstrate that Cupriavidus necator can serve as a robust and flexible platform for generating isotopically enriched biomolecules compatible with eukaryotic protein expression, thereby enabling NMR investigations of disease-relevant protein targets.

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Journal
Journal of Biomolecular NMR
Published
2026-02-25
DOI
https://doi.org/10.1007/s10858-026-00489-y
Primary Topic
Protein Structure and Dynamics
Type
article
Field-Weighted Citation Impact
0.00

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article

Cupriavidus necator, an alternative source for isotopic enrichment of proteins expressed in insect cells for NMR investigations

Krishna Saxena, Hermann Heumann, Harald Schwalbe, Fiona Rupprecht et al.
Journal of Biomolecular NMR
Protein Structure and Dynamics
article

Cupriavidus necator, an alternative source for isotopic enrichment of proteins expressed in insect cells for NMR investigations

Krishna Saxena, Hermann Heumann, Harald Schwalbe, Fiona Rupprecht, Sridhar Sreeramulu, S.L. Gande, Julian David Langer
article en

Abstract

Isotopic enrichment of pharmacologically relevant protein targets is crucial for structural studies by nuclear magnetic resonance (NMR) and plays a key role in advancing structure-guided drug discovery. Many clinically important drug targets require expression in eukaryotic systems-such as mammalian, yeast, or insect cells-rather than prokaryotic hosts. This requirement limits the feasibility of high-throughput isotopic labeling and poses challenges for obtaining uniformly isotope-labeled proteins suitable for NMR analysis. While several enrichment strategies have been developed, no broadly applicable enrichment platform has emerged for eukaryotic expression systems. In this study, we introduce Cupriavidus necator as an alternative biological source for <sup>15</sup>N and <sup>13</sup>C isotopic enrichment to support protein production in eukaryotic systems. To evaluate this approach, we selected the kinase domain of EPHA2, a receptor tyrosine kinase implicated in colorectal cancer progression and an important target for therapeutic inhibitor development. Isotopic incorporation was quantified using liquid chromatography-mass spectrometry (LC-MS), revealing enrichment levels of 79% for <sup>15</sup>N and 69% for <sup>13</sup>C. These results demonstrate that Cupriavidus necator can serve as a robust and flexible platform for generating isotopically enriched biomolecules compatible with eukaryotic protein expression, thereby enabling NMR investigations of disease-relevant protein targets.

Journal of Biomolecular NMRVol. 80(1)
Ceres (US), MRB Research Center for Magnetic Resonance Bavaria (DE), Max Planck Institute of Biophysics (DE), Max Planck Institute for Brain Research (DE), St. John's College (US), Thermo Fisher Scientific (Germany) (DE)
Deutsche Forschungsgemeinschaft
Good health and well-being
Openalex Percentile: Top 43%
Protein Structure and Dynamics
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