Details

Project TitleIn-Source Atmospheric Pressure-Electron Capture Dissociation (AP-ECD)
Track Code09-144
Short DescriptionA New Tool for Mass Spectrometric Analysis of Peptides and Proteins
AbstractNone
 
Tagsbioinformatics, cellular communications, drug research, health & life sciences, infectious disease, medical sciences, microbiology, science & technology
 
Posted DateDec 2, 2009 10:04 AM

Description

The technology is a new, practical, in-source atmospheric pressure (AP)-ECD method, that is suitable for use with mass spectrometers not otherwise equipped with ECD or ETD capabilities. The method utilizes a commercial atmospheric pressure photoionization (APPI) source, in conjunction with a novel nebulizer to provide electrospray-like ionization capabilities.

State of Development

Early results demonstrate that high quality ECD spectra can be acquired using a conventional Q-ToF mass spectrometer, to collect fragmentation information complementary to that of CID on an instrument where this was not previously possible.

Background

                Characterization of both the primary sequence and the post-translational modifications (PTMs) of peptides and proteins are central activities in diverse areas of biomedical research. Due to their lability PTMs are difficult to characterize using standard mass spectrometry fragmentation techniques.  Electron Capture (ECD) and Electron Transfer Dissociation (ETD) have emerged as powerful mass spectroscopic techniques for probing PTMs. Both ECD and ETD are normally performed using sophisticated, late-model ion trapping instruments, which have only recently become commercially available. Hence, the vast majority of the mass spectrometers used for protein/peptide analysis worldwide were not originally designed to perform either ECD or ETD, seriously restricting their utility in the analysis of PTMs.

Advantages

The device is suitable for coupling to any suitable mass analyzer, and may be retrofit to existing spectrometers. Thereby providing a low-cost option for ECD experiments and characterization of PTMs.

Sensitivity compatible with routine proteomic sequencing experiments

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