High-accuracy Temperature-controlled Electrospray Ionization Source for Characterization of Heat-induced

This technology provides a temperature-controlled electrospray ionization (ESI) source that allows for highly precise and accurate characterization of the thermal stability and aggregation of proteins by ESI mass spectrometry (MS). The ESI source was designed to eliminate artifacts that interfere with the detection of temperature-induced changes of biopolymer properties. It minimizes biopolymer degradation prior to the analysis, and incorporates a long heat shield to greatly improve thermal control during sample introduction into the ESI interface. This technology, coupled with high specificity of MS detection, enables the study of both reversible and irreversible processes of biopolymers in solution, and allows the early stages of heat-induced protein aggregation to be characterized in detail by monitoring both conformational changes and formation of oligomeric complexes as a function of temperature.

• New ESI source design strategies that prevent heat loss, protein degradation, and acidification of protein solution
• Adjustable sample flow rate allows process triggered by heat stress to be monitored in a time-resolved fashion
• Highly precise and accurate characterization of protein unfolding and aggregation

• Reversible unfolding of proteins
• Irreversible unfolding and aggregation of proteins
• Kinetic measurements of protein aggregation

Dr. Igor A. Kaltashov is a Professor in the Department of Chemistry and an expert in the field of biological mass spectrometry. His research is focused on developing mass spectrometry-based strategies to study biomolecular architecture, dynamics and interactions, and applying these techniques to the characterization of higher order structure and dynamics of protein therapeutics and other biopolymers.