![]() ![]() This attenuation is due to the interaction between the light and vibrational transitions in the covalent bonds of the molecules present in the sample. With this technique, the attenuation of an infrared light beam is measured when it passes through a sample. The aim of this work was to develop an innovative methodology to analyze the stability of therapeutic proteins based on FTIR spectroscopy. Moreover, infrared spectroscopy allows researchers to analyze these parameters in a precise, quick, and direct manner (i.e., giving results in a couple of minutes), with limited sample volume (<50µL) and without the need for extensive sample pre-treatment or the requirement to recalibrate on each measurement day. Depending on specific situations, gathering these data would typically require leveraging three to four distinct techniques and protocols. In this article, the authors demonstrate the feasibility of simultaneously obtaining information regarding four key characteristics of therapeutic proteins: structural integrity, overall protein concentration, quantification of glycosylations, and quantification of phosphorylations. Harnessing the strengths of Fourier transform infrared spectroscopy (FTIR) and recent improvements in chemometrics, new analytical methods have been developed to study the stability and perform comparability studies of therapeutic proteins. Yet, the inherent complexity of proteins requires the development of new analytical strategies to characterize and ensure the quality and safety of these products. Rapid commercialization of therapeutic proteins remains a challenge notably due to their chemical and physical instabilities. ![]()
0 Comments
Leave a Reply. |
AuthorWrite something about yourself. No need to be fancy, just an overview. ArchivesCategories |