GEN-MKT-18-7897-A
Sep 17, 2021 | Biopharma, Blogs | 0 comments
Read time: 3 Minutes
A powerful combination: The Zeno trap and electron activated dissociation (EAD) fragmentation Sensitivity is a fundamental performance characteristic of a mass spectrometer. Increasingly higher sensitivities are in constant demand in order to characterize and quantify analytes that are at an ever decreasing abundance.
Electron activated dissociation or EAD is a ground-breaking approach for tandem mass spectrometry applications. While the industry standard collision induced dissociation (CID) has proven to be an invaluable tool for MS/MS experiments, the data produced using CID can leave gaps.
Together the Zeno trap and EAD fragmentation are a powerful combination.
You can now discover new levels of control, with a step change in fragmentation technology. You have the ability to create reproducible fragmentation patterns through high-energy collisions (CID) or, precisely disassemble molecules, exploring new perspectives. You will be able to fine tune fragmentation energies, allowing controlled electron-activated dissociation of all molecule types.
These advanced fragmentation mechanisms create a myriad of insight within your reach. Zeno trap pulsing unlocks extraordinary sensitivity gains, uncovering information that has always existed undetected, adding new perspective to your quantitative and qualitative data.
Together the Zeno trap and EAD provide the ability to acquire key MS/MS features needed to:
The Zeno trap: The next era of sensitivity for accurate mass
Ions are accumulated in the Zeno trap before being pulsed rapidly into the TOF, meaning up to 20x more ions can be detected. Consequently, each TOF experiment contains more useful MS/MS information, particularly on lower abundance species that were previously undetectable, introducing our customers to a new level of sensitivity.
Electron activated dissociation (EAD): A step change in fragmentation technology The ability to tune electron kinetic energy extends the utility of the approach to all molecule types from singly charged small molecules to large multiply charged proteins. EAD allows for a range of reagent free electron-based fragmentation mechanisms within one device, and has the capability to fragment peptides whilst retaining critical MS/MS information for both identification and localization of PTMs. Unlike other electron based fragmentation techniques, EAD delivers reproducible, consistent data, even at fast scan speeds, compatible with UHPLC timeframes, delivering higher efficiency than ETD.
A revolution in accurate mass has arrived. The ZenoTOF 7600 high-resolution accurate mass system combines the power of Zeno trap pulsing with EAD fragmentation which allows for detection of very low abundant diagnostic fragment ion species leading to greater sequence coverage.
Now, you can watch as rare data becomes your everyday and your toughest challenges become your greatest advantage. Now, new discovery is not only possible, but quantifiable.
Welcome to the Zeno revolution.
Related to: RUO-MKT-19-13372-A, RUO-MKT-19-13373-A, RUO-MKT-18-13402-A and RUO-MKT-17-13406-A
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As an analytical strategy, middle-down mass spectrometry (MS) workflows characterize biotherapeutic proteins by analyzing large, digested protein fragments or defined subunits, rather than fully intact proteins (top-down) or digested peptides (bottom-up). A middle-down strategy combines the strengths of top-down and bottom-up approaches by delivering high sequence coverage and structural specificity while maintaining relatively simple sample preparation. In practice, middle-down analysis enables accurate mass measurement, rapid sequence confirmation, and localization of key post-translational modifications (PTMs) on protein subunits that are directly relevant to product quality.
In biopharmaceutical development, sequence variants (SV) are considered an inherent risk of producing complex proteins in living systems. Sequence variants are unintended changes to the amino acid sequence of a biotherapeutic and can be caused by errors in transcription or translation in the host cell, or cell culture and process conditions. Detailed analysis of SVs is important in process and product development to ensure the drug’s safety and efficacy. Even low‑level sequence variants can have significant implications for product quality, safety, and efficacy, making their accurate detection and characterization a critical requirement across development, process optimization, and regulatory submission.
CE‑SDS remains a cornerstone assay for characterizing fragmentation, aggregation, and product‑related impurities in therapeutic proteins. UV detection has been the long‑standing standard. However, it frequently struggles with baseline noise, limited sensitivity for minor fragments, and subjective integration.
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