Agilent announces the immediate availability of the ExD AQ-250 Option, which provides a new, powerful, and easy-to-use electron-based fragmentation technology that is a field-installed enhancement for the 6545-6560 family of Q-TOFs. The e-MSion ExD AQ-250 Option makes possible far more complete characterization of proteins and glycoproteins with unprecedented accuracy, speed and simplicity. The ExD AQ-250 Option is comarketed with e-MSion Inc located in Corvallis, Oregon. The technology has been developed through a ten-year collaborative effort with Agilent.
The ExD AQ-250 Option is available for both new Agilent instruments or can be retrofitted into recent existing Q-TOF mass spectrometers. The ExD AQ-250 Option is a drop-in replacement for the Agilent collision cell that offers superior electron fragmentation in combination with collision induced dissociation (CID) to produce more reliable identification of larger peptides and proteins than previously possible. The original functionality, sensitivity, and resolution of the Q-TOF are preserved and the ExD can be automatically optimized with Agilent’s SWARM optimization.
The ExD cell is the only electron-based technology that fast enough to fragment proteins after with ion mobility separation (IMS). When installed on Agilent’s 6560 Ion Mobility Q-Tof, the ExD AQ-250 Option gives provides unprecedented and unique abilities to probe protein conformation after separation by ion mobility.
e-MSion’s ExD technology fragments proteins in precise and predictable ways in common with electron transfer dissociation (ETD). ExD fragmentation is simpler because no trapping is needed with a negatively charged ETD reagent. The major advantage of ExD over ETD is the ability to activate analyte ions before, during and after electron capture using CID. As a result, the ExD cell produces higher coverage of native proteins up to 25-30 kDa than possible with other commercially available fragmentation techniques and with more simplicity.
Unlike ETD, the ExD technology can produce higher energy electrons to fragment across more complex ring structures to give better characterization of glycans. In addition, ExD induces side chain fragmentation that can differentiate isobaric leucine from isoleucine, and to provide better mapping disulfide chains. The ExD cell also readily distinguishes isoaspartate from aspartate and other degradation products affecting biopharmaceutical quality.
The ExD technology preserves labile post-translational modifications on large peptides and intact proteins, which allows for the simultaneous quantitation of multiple phosphorylation and glycation sites in bottom-up and middle down proteomic work flows.
The superior dissociation of native proteins by ExD with retention of post-translational modifications and side chain differentiation opens new opportunities for more complete characterization of complex proteoforms in a highly cost-effective platform.
