Stability and homogeneity of therapeutic antibodies are of primary concern due to the effect on safety and efficacy. Undesired biochemical, structural and conformational forms can lead to a loss of potency or, in the worse-case, severe adverse side effects. As such, the evaluation of disulfide bonds is an important aspect of gaining a comprehensive understanding of the chemical structure of a protein.
DisulfideDetect software is a quantum leap in ease-of-use for detecting and evaluating disulfide bonds within therapeutic proteins, such as monoclonal antibodies. It provides an easy to understand, visually-based, workspace for disulfide bond analysis for both native and non-native bonds as well as inter- and intra-chain disulfide bonds within the protein/antibody.
The tertiary structure of therapeutic proteins is key to their activity and stability. Due to the complexity of these proteins and the fact that they will contain multiple disulfide bonds, analysis is a challenge – often requiring several LC/MS runs with the tryptic digests from reduced and non-reduced protein and a manual comparison of these two analyses.
The DisulfideDetect workflow allows the fully automated analysis of disulfide bonds in biopharmaceuticals, based on a single digest of the unreduced protein and without prior knowledge of enzyme specificity or native disulfide bonds. The workflow provides a semi-quantitative scrambling analysis as well.