Pharma & Biopharma

In this report, we illustrate the utility of calorimetry in making better laboratory decisions. Examples will include improved protein construct selection for scale-up; direct measurement of the effects of mutations and post-translational modifications on protein stability; rapid optimization of solvent formulation; direct measurement of substrate and inhibitor binding affinity; determination of the mode of inhibitor binding; characterization of protein-protein interactions; and improved structural biology efficiency, when used in conjunction of other biophysical methods.

Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies Choosing the best antibody to progress in your biologic pipeline. Temperature-induced unfolding of three humanized IgG1 monoclonal antibodies and their Fab and Fc fragments was monitored by differential scanning calorimetry at neutral pH. With some exceptions, the thermogram of the intact antibody presents two peaks and the transition with the larger experimental enthalpy contains the contribution from the Fab fragments. Although the measured enthalpy was similar for all three Fab fragments studied, the apparent melting temperatures were found to vary significantly, even for Fab fragments originating from the same human germline.

See how you can use DSC to save you money in your contract development lab. This paper provides an overview of the workflow typically associated with preformulation projects at a contract development organization as well as provides a general framework for conducting preformulation studies that leverages the application of biophysical techniques such as DSC and traditional analytics by employing statistical design. A case study involving the formulation development of a monoclonal antibody is presented to detail the utility and potential limitations of DSC in support of preformulation for a variety of protein products.

This four-part series examines common issues and questions surrounding the principles, measurements and analysis of DLS data and discusses how to minimize the time required for and increase the accuracy of acquiring and interpreting DLS data during the biotherapeutic development process. In Part Four, we address frequently asked questions related to the application of DLS to the characterization of protein therapeutic formulations.

This four-part series examines common issues and questions surrounding the principles, measurements and analysis of DLS data and discusses how to minimize the time required for and increase the accuracy of acquiring and interpreting DLS data during the biotherapeutic development process. In Part Three, we cover the basic types of DLS deconvolution algorithms used to extract the intensity weighted particle size distribution from the measured correlogram.

This four-part series examines common issues and questions surrounding the principles, measurements and analysis of DLS data and discusses how to minimize the time required for and increase the accuracy of acquiring and interpreting DLS data during the biotherapeutic development process. In Part Two, we cover the influence of concentration effects and particle interactions on DLS results and provide a roadmap for identifying and distinguishing each type of concentration effect.

This four-part series examines common issues and questions surrounding the principles, measurements and analysis of DLS data and discusses how to minimize the time required for and increase the accuracy of acquiring and interpreting DLS data during the biotherapeutic development process. In Part One, we provide an overview of the key principles of DLS: theory, correlation statistics, deconvolution algorithms, and the intensity to mass transform.

Use of a novel combination of dynamic light scattering and Raman spectroscopy to elucidate the conformational stability and structure of proteins in biopharmaceutical formulations

The role that nanoparticles play in the rapidly developing field of ‘NanoMedicine’ has been discussed previously in Chapter 5. In this Chapter, we review the specific mechanisms by which such nanoparticles are designed and formulated and in which NTA has had a significant part to play.

The combination of static microscopy and Raman spectroscopy in the Morphologi G3-ID enables automated chemical identification of protein aggregates and other contaminants in a biotherapeutic sample, either in suspension via a thin-path wet cell or on a filter membrane.