Protein Binding Studies
A detailed understanding of protein binding interactions is an integral part of biologic drug discovery and development activities. QuarryBio’s labeling technology is able to identify specific residues involved in binding interactions for essentially any protein.
- Epitope mapping – identifies the binding location on the antigen. Multiple proteins can be measured against a single antigen to support binning activities, allowing greater precision when selecting proteins to advance during hit-to-lead selection.
- Paratope mapping – identifies the binding location on the biologic drug being studied. Both epitope and paratope mapping can be performed in isolation or simultaneously, depending on the client’s request.
The biological function of therapeutic proteins is largely determined by their 3-dimensional structure. QuarryBio’s labeling technology enables our clients to identify, compare, and quantify changes in protein 3-dimensional structure with high resolution. This not only allows for direct comparison of protein structure across a wide range of discovery, development, and commercial activities, but can also improve our client’s understanding of the relationship between protein structure and the conditions being explored.
- Stability studies – stability studies are a primary means of ensuring that only the most robust drug candidates and formulations are selected for advancement. QuarryBio’s labeling technology not only has a higher sensitivity than commonly used analytical methods (CD, fluorescence, DLS, etc.), but also delivers information regarding specific residues in the protein that are most impacted. This provides researchers with new insights into the structural impacts of stress conditions, informing both protein engineering and formulation development improvement efforts.
- Comparability studies – developing, scaling up, manufacturing, and storing/shipping proteins entail activities that can all have an unintended impact on the 3-dimensional structure of proteins. Opportunities for improvement for any of these activities, as well as unexpected adverse events, must be evaluated for potential impacts on protein structure. Comparability studies are a common way to ensure that proteins do not change in undesirable ways in response to any of these activities. QuarryBio’s Covalent Labeling technology offers an innovative and unique way to provide a high resolution comparison of the protein 3-dimensional structure before and after the change being evaluated. Our method can not only identify changes in the structure, but information regarding the location of the change in the structure can provide valuable insight into the causes and impact of these changes in regard to protein safety and efficacy.
- Biosimilars – the introduction of generic competition for biotechnology products presents many significant challenges, including the identification of methods to provide high resolution comparisons of the structure of the proposed biosimilar to the branded original. QuarryBio’s Covalent Labeling method not only provides a high resolution comparison of the 3-dimensional structures, but also where in the structure variations exist. This provides critical information for the developers of biosimilar as they optimize their product to more exactly match the bio-originator structure.