Boston University School of Medicine and Bruker Establish a Collaborative Effort in Glycomics and Advanced FTMS Applications
August 03 2009 - 7:00AM
Business Wire
Bruker Daltonics announced today that it has established a
collaboration with the Mass Spectrometry Resource laboratory of
Professor Catherine Costello at the Boston University School of
Medicine (BUSM). The collaborative effort will focus on the
application of high performance ion trap mass spectrometry and
Fourier Transform Mass Spectrometry (FTMS) to glycomics and
proteomics applications. The researchers at the Boston University
School of Medicine are already using the recently introduced Bruker
amaZonTM ion trap mass spectrometer for detailed and high
throughput analyses of glycan structures, and have just ordered a
solariXTM FTMS with a 12 Tesla magnet for high performance
bottom-up and top-down proteomics and glycomics with ETD and ECD
capabilities.
Professor Costello is a Research Professor of Biochemistry,
Biophysics and Chemistry, and the Director of the BUSM Center for
Biomedical Mass Spectrometry. Her laboratory is a resource center
sponsored by the NIH where mass spectrometry is applied to the
study of biopolymers (proteins, carbohydrates and lipids) by local,
national and international collaborators. The recent award of an
NIH-NCRR High-End Shared Instrumentation Grant to the BUSM Center
provided the funds for purchase of the solariX. Professor
Costello and her group are recognized internationally as experts in
the analysis of the complex structures of carbohydrates and their
conjugates, such as glycoproteins and glycolipids. While these
important classes of molecules are involved in immune system
recognition, nervous system development, and many other critical
biological processes, methods for their full structural
characterization are less developed than for linear biopolymers
such as proteins and oligonucleotides. Not only are the structures
of carbohydrates more complex, because of their non-linear,
branched structures, but they usually occur in complex
mixtures.
The recently introduced Bruker solariX FTMS provides the
highest mass resolving power and mass accuracy available on any
mass spectrometer, making it ideally suited to tackle extremely
complex mixtures. Additionally, the solariX offers the most
versatile suite of tools for fragmenting biopolymers, including
Collision Induced Dissociation (CID), either in the front-end
collision cell and/or in the ICR cell, as well as Electron Capture
Dissociation (ECD) in the ICR cell, and now even front-end Electron
Transfer Dissociation (ETD). All of these structural tools are
further augmented by the novel geometry of the solariX
system that enables Continuous Accumulation of Selected Ions
(CASI™) for selectively enriching low abundant signals from
specifically chosen carbohydrates, peptides or proteins.
The use of top-down and bottom-up proteomics techniques on the
FTMS allows for rapid structural characterization of proteins and
the discovery of Post-Translational Modifications (PTMs), including
the glycosylation sites of particular interest to Professor
Costello’s group. Bruker Daltonics and Professor Costello’s
research group will work together to develop new workflows and
approaches for high performance LC-FTMS/MS, using CID, ETD and ECD,
for proteomics and glycomics research.
The Bruker amaZon ion trap offers unsurpassed ion trap
speed and sensitivity including routine operation in MS3, up to 10
stages of MS/MS and a unique ultra-high sensitivity implementation
of ETD. The speed and sensitivity of the amaZon, together
with fast MSn and ETD make it an ideal tool for obtaining in-depth
structural information on complex carbohydrate structures. Prof.
Cathy Costello and Bruker Daltonics also plan to collaborate on the
development of new methods for structural analysis of
carbohydrates, such as the recently developed, “reverse” ETD
(r-ETD), in which negatively charged carbohydrate ions with
multiple charges are reacted with a positively charged reagent ion
to induce fragmentation. This is an important development as
ionization of carbohydrates is often much more efficient in
negative ion mode, and the normal ETD process will not work with
negative analyte ions.
Professor Cathy Costello commented: “We and our collaborators at
the Boston University School of Medicine are already excited about
the excellent results being obtained from the amaZon
instrument. We now look forward to the delivery of the
solariX FTMS system. Bottom-up and top-down proteomics
studies on the solariX FTMS will enhance our capabilities
for the discovery of novel PTMs, including glycosylation. The
availability of ETD, r-ETD, ECD, and multiple stages of CID MS/MS
will greatly enhance our capabilities for the structural analysis
of novel carbohydrate structures.”
“We are delighted that Professor Costello, who has an
outstanding record in the development of mass spectrometry for new
applications in the study of carbohydrates, has chosen Bruker as a
partner in developing further applications of glycomics,” stated
Dr. Paul Speir, Bruker Daltonics’ Vice President for FTMS. “We view
our solariX ESI-FTMS with high field magnets as the ultimate
platform for the characterization of complex mixtures and the
structural analysis of the components of such mixtures. Further
collaborative development of the amaZon as a
high-throughput, high-performance research tool for the structural
analysis of complex carbohydrates, and the collaboration on the
optimization of both ETD and r-ETD methods for glycan analysis,
make this a very exciting and important research collaboration for
Bruker.”
ABOUT BRUKER DALTONICS
For more information about Bruker Daltonics and Bruker
Corporation (NASDAQ: BRKR), please visit www.bdal.com and
www.bruker.com.
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