Understanding disulfide bonding is critical for protein characterization and in helping solve the structure. Incorrect disulfide bond formation or exchange can be side-effects of longterm mAb storage that can cause antibody aggregation. Providing early insight into the integrity of a biotherapeutic can allow identification of potential sources of error early on. Disulfide bonds can contribute to aggregation and must be monitored in regards to patient safety. In the biopharmaceutical production, elucidating the cysteine connectivities is necessary to prevent disulfide scrambling and folding incorrectly. Our services are typically used to Identify the number and/or position of disulfide bridges present or to detect mismatched or scrambled disulfide bridge formation.
Mass spectra are compared before and after digestion to determine the location and type of disulfide bond present. DTT reduction is used to determine if the bond is inter-peptide or intra-peptide. Additionally, patterns within the spectra can be used to positively identify the presence of disulfide bonding.