Disulfide Bond Mapping in Recombinant Protein Drugs

Recombinant protein drugs are a class of medications where proteins serve as the primary active ingredient. These drugs typically have a molecular weight significantly greater than that of traditional small molecule drugs, and their structures are more complex. Recombinant protein drugs can directly interact with molecular mechanisms within the body, offering high specificity, robust biological activity, and relatively low side effects. Some recombinant protein drugs are copies of naturally occurring biomolecules, such as insulin or growth hormone. These medications can replace or supplement the natural proteins that are deficient in the body, thereby alleviating symptoms. Other recombinant protein drugs, such as monoclonal antibodies, are artificially designed using genetic engineering techniques to specifically target and neutralize disease-related molecules.

 

In recombinant protein drugs, disulfide bonds play a crucial role in the stability, folding, and functionality of the protein structure. During the development of biopharmaceuticals, accurate detection and control of disulfide bonds in proteins is essential. Incorrect disulfide bond pairing can lead to drug ineffectiveness and may pose potential safety risks. Current methods for disulfide bond mapping primarily include mass spectrometry, nuclear magnetic resonance, X-ray crystallography, and chemical-assisted techniques.

 

Mass spectrometry is a commonly used method for disulfide bond mapping, known for its high sensitivity and resolution. This technique involves cleaving recombinant protein drugs into peptide fragments using specific enzymes or chemical reagents, followed by mass spectrometric analysis of these fragments. This allows for the direct measurement of the masses of the protein fragments, thereby determining the positions of disulfide bonds. Additionally, mass spectrometry can handle relatively large sample sizes and has lower purity requirements for the samples.

 

MtoZ Biolabs provides high-level solutions for disulfide bond analysis of protein drugs through their high-resolution mass spectrometry technology services, combined with years of experimental experience. This includes methods for blocking protein disulfide bond in vitro exchange, maintaining its natural structure sample preparation method, disulfide bond cross-linked peptide segment mass spectrometry analysis method, and supporting disulfide bond identification pLink-SS software analysis. It can achieve disulfide bond connection and free thiol analysis. Disulfide bond connection can confirm the number and position of disulfide bonds in recombinant protein drugs through mass spectrometry. Through years of experience, MtoZ Biolabs can efficiently detect regular disulfide bonds, cross-overlapping disulfide bonds, or mismatched disulfide bonds.