ArticleJournal of biomolecular NMR2021
Detecting aspartate isomerization and backbone cleavage after aspartate in intact proteins by NMR spectroscopy.
Article in Journal of biomolecular NMR, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- A Combined Experimental-Theoretical Approach Unveils the Comprehensive Asn Deamidation Kinetics.Journal of the American Chemical Society · 2026Article
- Advanced NMR Characterization and Sensitive Detection of Isoaspartate in Proteins.Analytical chemistry · 2026Article
- Phage Display Technology: Design, Library Construction, and Panning Strategies for Antibody Development.Biomolecules & therapeutics · 2026Review
- The NMR signature of maltose-based glycation in full-length proteins.Journal of biomolecular NMR · 2024Article
- Nonenzymatic Posttranslational Modifications and Peptide Cleavages Observed in Peptide Epimers.Journal of the American Society for Mass Spectrometry · 2023Article
- Unambiguous Identification of Glucose-Induced Glycation in mAbs and other Proteins by NMR Spectroscopy.Pharmaceutical research · 2023Article
- Synthesis of Novel Carborane-Containing Derivatives of RGD Peptide.Molecules (Basel, Switzerland) · 2023Article
- Fundamental Clock of Biological Aging: Convergence of Molecular, Neurodegenerative, Cognitive and Psychiatric Pathways: Non-Equilibrium Thermodynamics Meet Psychology.International journal of molecular sciences · 2021Review
- Expression of acid cleavable Asp-Pro linked multimeric AFP peptide in E. coli.Journal, genetic engineering & biotechnology · 2021Article
- Unambiguous identification of α-Gal epitopes in intact monoclonal antibodies by NMR spectroscopy.mAbsArticle
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The monitoring of non-enzymatic post-translational modifications (PTMs) in therapeutic proteins is important to ensure drug safety and efficacy. Together with methionine and asparagine, aspartic acid (Asp) is very sensitive to spontaneous alterations. In particular, Asp residues can undergo isomerization and peptide-bond hydrolysis, especially when embedded in sequence motifs that are prone to succinimide formation or when followed by proline (Pro). As Asp and isoAsp have the same mass, and the Asp-Pro peptide-bond cleavage may lead to an unspecific mass difference of + 18 Da under native conditions or in the case of disulfide-bridged cleavage products, it is challenging to directly detect and characterize such modifications by mass spectrometry (MS). Here we propose a 2D NMR-based approach for the unambiguous identification of isoAsp and the products of Asp-Pro peptide-bond cleavage, namely N-terminal Pro and C-terminal Asp, and demonstrate its applicability to proteins including a therapeutic monoclonal antibody (mAb). To choose the ideal pH conditions under which the NMR signals of isoAsp and C-terminal Asp are distinct from other random coil signals, we determined the pK
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.