Join us to celebrate the achievements of the 60 impactful analytical scientists featured in the 2024 Power List.
11/17/2015 | Tiemin Huang
Coupling whole column imaging detection to a mass spectrometer for protein structure characterization is fundamentally challenging. Could a relatively simple capillary cartridge system unlock the potential?
11/16/2015
To formulate successfully with HA it is essential to understand the impact of factors such as molecular weight, molecular structure, concentration and degree of cross-linking on rheological characteristics such as viscoelasticity which are directly linked to aspects of product performance. Linking structural characteristics to product performance, via rheological properties, supports smart, fast, and effective formulation. The following study shows how rheology and particle size measurements can be used to characterize the physical properties of HA dermal fillers.
Polyol-induced increases in thermal stability of antibodies. See how Differential scanning calorimetry can be used to assess the effects of polyol excipients on antibodies. DSC was used to monitor polyol-induced increases in thermal stability across seven monoclonal antibodies. The increases in thermal stability were measured as a function of polyol concentration and orientation of hydroxyl groups. It was found that increases in thermal stability were linear with respect to alcohol concentration.
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.
11/16/2015 | Rich Whitworth
Kickstarter technology is nothing new – but Clear Labs is making in-roads into something less common: kickstarter analytical science
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.
10/20/2015 | Alexander Makarov
Coupling gas chromatography with Orbitrap™ technology wasn’t easy, but the outcome – the introduction of the Thermo Scientific Q Exactive™ GC – represents a big step towards bringing full-scan, high-resolution, and accurate mass data into routine labs around the world. And my dream of an “Orbitrap in every lab” inches ever closer.
10/19/2015 | Victoria Barton
Sniffing out ‘off smells’ in drinking water with a bioelectronic sensor
10/15/2015
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.
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