Post-Translational Modifications of Protein Drugs
With the development of biopharmaceutical technology, an increasing number of protein-based drugs are being developed for the treatment of various diseases. Common protein-based drugs include proteins, peptides, monoclonal antibodies, vaccines, and antibody-drug conjugates. These protein drugs sometimes require modifications to exert the intended biological function and achieve therapeutic effects. Common post-translational modifications of protein drugs include glycosylation, disulfide bonds, acetylation, and phosphorylation. Different types of modifications, amino acid modification sites, and modification levels can significantly impact the safety and efficacy of the final drug product. Studies have shown that the degree of glycosylation is closely related to the activity and half-life of erythropoietin (a protein drug), and the type of glycan chains in monoclonal antibodies affects their affinity with receptors. Therefore, the analysis and identification of post-translational modifications of protein drugs are essential. Currently, liquid chromatography-tandem mass spectrometry (LC-MS/MS) is primarily used for the identification of post-translational modifications of protein drugs, with principles and analytical processes similar to conventional protein post-translational modification identification.
Biotech company Bio-Techne utilizes Thermo Fisher's Q Exactive HF mass spectrometry platform combined with Nano-LC chromatography to provide fast and efficientproteindrugpost-translational modification identificationservice package. You only need to inform us of your experimental objectives and send us your samples. We will handle all subsequent project matters, including protein extraction, proteolysis, modified peptide enrichment, peptide separation, mass spectrometry analysis, mass spectrometry raw data analysis, and bioinformatics analysis. Free consultations are welcome.
Related services:
Post-translational modification proteomics analysis
Acetylation quantitative proteomics study
Phosphorylation quantitative proteomics study
Ubiquitination quantitative proteomics study
Glycosylation quantitative proteomics study
Protein disulfide bond identification and quantitative analysis
Histone post-translational modification analysis
Multipathway phosphorylation proteomics
Methylation quantitative proteomics study
Acylation quantitative proteomics study
Protein SUMOylation identification
Characterization of PTMs based on Top-down approach
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