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Articles
Native Measurement of a Biotherapeutic without Interference from Excipients Using Microfluidic Modulation Spectroscopy
August 1, 2019
Spectroscopy North America
Jeffrey Zonderman, Libo Wang, Ioannis A. Papayannopoulos, Shannon Renn-Bingham
A new infrared spectroscopy technique, microfluidic modulation spectroscopy (MMS), delivers reproducible protein characterization over close to four orders of magnitude in protein concentration (from 0.1 to 200 mg/mL). This technique characterizes samples from the earliest stages of development through to manufacture.
A defining requirement in biopharmaceutical development, formulation, and manufacturing is to elucidate and maintain the structure of the drug entity. That work relies on relevant protein characterization, a task complicated by how samples evolve through the drug development lifecycle. The requirement to change techniques to cope with progressively more concentrated, and complex, multicomponent formulations is a major issue when it comes to comparing datasets and safeguarding structural parity. In this article, we discuss a new infrared spectroscopy technique, microfluidic modulation spectroscopy (MMS), that delivers reproducible protein characterization over close to four orders of magnitude in protein concentration, from 0.1 to 200 mg/mL. This technique can transition with the sample from the earliest stages of development through to manufacture, and present experimental data demonstrating the concentration-independent data that can be generated.
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