ReviewAnalytical and bioanalytical chemistry2018
Recent mass spectrometry-based techniques and considerations for disulfide bond characterization in proteins.
Review in Analytical and bioanalytical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Experimental Detection Methods and Clinical Translational Challenges of Disulfidptosis in Cancer.Cells · 2026Review
- Engineering a Second Interchain Disulfide Bond in the αβ T-Cell Receptor Constant Domain: A Powerful Strategy to Enhance Stability, Pairing Fidelity, and Therapeutic Efficacy in TCR-T Cell Therapy.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Impact of Supercharging on Top-Down Characterization of Monoclonal Antibodies by Collision Induced Dissociation.International journal of mass spectrometry · 2026Article
- Disulfide Bond Mapping of Follitropin Delta, a Recombinant Follicle Stimulating Hormone (rFSH), by X-Ray Crystallography.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Assessment of Peanut Allergen Cross-Contact Risk from Reused Roasting Oil Using a Targeted Proteomics Method.Journal of agricultural and food chemistry · 2026Article
- Identification of Target Disulfide Bonds Using Mechanism-Based Kinetic Trapping Combined with Differential Cysteine Labeling.Methods in molecular biology (Clifton, N.J.) · 2026Article
- A novel recognition of the major allergen, Hum j 1, fromThe World Allergy Organization journal · 2025Article
- High-Performance Structures of Biopolymer Gels Activated with Scleroprotein Crosslinkers.Molecules (Basel, Switzerland) · 2025Article
- Analysis of multi-disulfide bridges for insulin aspart by stepwise reduction and differentiated alkylation.Analytical and bioanalytical chemistry · 2024Article
- Transient Conformations Leading to Peptide Fragment Ion [c + 2H]Molecules (Basel, Switzerland) · 2023Article
- Thiol redox proteomics: Characterization of thiol-based post-translational modifications.Proteomics · 2023Review
- Legumain Functions as a Transient TrkB Sheddase.International journal of molecular sciences · 2023Article
- Comprehensive investigation of a structural variant in a bi-specific, N-and C-terminal Fc-fusion molecule, and its monitoring with LC-MS based method.Biotechnology and bioengineering · 2023Article
- Article
- Multienzyme deep learning models improve peptide de novo sequencing by mass spectrometry proteomics.PLoS computational biology · 2023Article
- Protein Digestion for 2D-DIGE Analysis.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Characterization of disulfide bridges pattern of recombinant human interleukin 12 fusion protein p40 subunit and identification and quantification of cysteinylated free cysteine 252.Rapid communications in mass spectrometry : RCM · 2022Article
- First report of computational protein-ligand docking to evaluate susceptibility to HIV integrase inhibitors in HIV-infected Iranian patients.Biochemistry and biophysics reports · 2022Article
- Mass Spectrometry-Based Disulfide Mapping of Lysyl Oxidase-like 2.International journal of molecular sciences · 2022Article
- Hidden Relationships betweenInternational journal of molecular sciences · 2022Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Disulfide bonds are important structural moieties of proteins: they ensure proper folding, provide stability, and ensure proper function. With the increasing use of proteins for biotherapeutics, particularly monoclonal antibodies, which are highly disulfide bonded, it is now important to confirm the correct disulfide bond connectivity and to verify the presence, or absence, of disulfide bond variants in the protein therapeutics. These studies help to ensure safety and efficacy. Hence, disulfide bonds are among the critical quality attributes of proteins that have to be monitored closely during the development of biotherapeutics. However, disulfide bond analysis is challenging because of the complexity of the biomolecules. Mass spectrometry (MS) has been the go-to analytical tool for the characterization of such complex biomolecules, and several methods have been reported to meet the challenging task of mapping disulfide bonds in proteins. In this review, we describe the relevant, recent MS-based techniques and provide important considerations needed for efficient disulfide bond analysis in proteins. The review focuses on methods for proper sample preparation, fragmentation techniques for disulfide bond analysis, recent disulfide bond mapping methods based on the fragmentation techniques, and automated algorithms designed for rapid analysis of disulfide bonds from liquid chromatography-MS/MS data. Researchers involved in method development for protein characterization can use the information herein to facilitate development of new MS-based methods for protein disulfide bond analysis. In addition, individuals characterizing biotherapeutics, especially by disulfide bond mapping in antibodies, can use this review to choose the best strategies for disulfide bond assignment of their biologic products. Graphical Abstract This review, describing characterization methods for disulfide bonds in proteins, focuses on three critical components: sample preparation, mass spectrometry data, and software tools.
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