BILLERICA, Mass.--(BUSINESS WIRE)--Aug. 3, 2009--
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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Source: Bruker Daltonics
Bruker DaltonicsDr. Gary Kruppa, +1 978-663-3660, ext. 1227Vice
President, Business Developmentgary.kruppa@bdal.com