In less than 5 minutes, a FTIR measurement can provide a spectrum representing a global and unique fingerprint of a sample’s composition. This sum of information is demonstrated to be very accurate and sensitive to subtle changes, but needs to be interpreted in such a way as to maximize the amount of information that can be retrieved.
Over the last 10 years, our team has developed the proprietary expertise, through one single FTIR measurement, to retrieve information on 4 key parameters related to protein structure and quantification:
higher order structure: absence of denaturation and aggregation;
composition and quantification of post-translational modifications: glycosylations, oxidation, phosphorylations,…;
absolute protein concentration and
quantification of key excipients such as detergents (Tween,…), stabilizing agents or lipids.
Depending on specific situations, gathering these data would require leveraging 3 to 4 distinct techniques and protocols today. Moreover, infrared spectroscopy allows to analyze protein structure and components in a precise, quick and direct manner (a couple of minutes), with limited sample volume (<50µg) and without need for extensive sample pre-treatment or recurring calibration. Speed of measurement can therefore be up to 3 to 10 times higher than with other techniques.