omation mbers - Society for Laboratory Automation and Screening

11:30 am Thursday, February 5 Proteomics – Technology 3 Room B1
Joseph Loo
University of California, Los Angeles
405 Hilgard Avenue, 402 MBI
Los Angeles, California 90095
jloo@chem.ucla.edu
A View of the Proteome Provided by New Mass Spectrometry Technologies
93
Co-Author(s)
Rachel R. Ogorzalek Loo
New technologies based on mass spectrometry (MS) and proteomics are being developed to address a number of
health-related applications. Parallel approaches that probe complex systems as a unit, rather than one component
at a time best allow for the understanding of protein expression per an organism’s developmental state and its
response to the environment. An MS-based surface scanning method has been developed in which proteins are
desorbed directly from 1D isoelectric focusing gels to create a virtual 2D gel; data are presented as an image,
similar to that obtained from a stained 2D gel. Beyond the improved mass accuracy and mass resolution provided
by substituting MS for SDS-PAGE, the virtual 2D gel has several advantages over the traditional 2D gel, including
high-speed analysis. Small differences between measured and predicted molecular weights can flag contributing
post-translational processing and protein modification. ESI-MS for studying noncovalent complexes has utility
in chemical biology and biomedical research. ESI has the ability to ionize macromolecules and maintain weak
noncovalent interactions. The mass measurement provides a direct determination of the stoichiometry of the
binding partners in the complex. In addition to identifying the components that are involved in protein interaction
networks, MS studies can identify and elucidate the geometry and interactions of protein machines, such as the
690 kDa proteasome, the protease responsible for protein degradation, and the 14 MDa vault, a ribonucleoprotein
particle implicated in multidrug resistance.
1:30 pm Thursday, February 5 Automation Applications in Process R&D Room A2
Norbert Stoll
University Rostock
R.-Wagner-Str. 31
Rostock, 18119 Germany
norbert.stoll@uni-rostock.de
Microreactor Systems for Life Science Application
Co-Author(s)
Arne Allwardt
Kerstin Thurow
The use of combinatorial methods in chemistry and life science has been developing rapidly within the last years.
Since there has been numerous developments in the field of pharmaceutical research in microtiter plate format
there is still a lack of suitable instruments for classical. combinatorial chemistry in the mL-range. Synthesis in drug
discovery or catalyst screening requires quite often high temperatures and high pressures as reaction condition for
hydration, carbonylation or oxidation. The often long reaction times requires parallelization of reactors in order to
increase the throughput. Existing instruments are not flexible automated solutions and do not have flexible material
and information interfaces. On the other hand they do not always meet the requirements from organic chemists.
To fill this gap an integrated automated system for organic high pressure synthesis had to be developed. The
presentation will give an overview about existing systems and will show current and future developments in the
field of organic high pressure synthesis. Two systems will be demonstrated for reactions in the mL-range (multi
parallel reactor array 8/16/24) and for reactions in the MTP-Format (96 / 384). The systems are high temperature/
high pressure designed. Both systems are integrated into an analytical environment to perform a coupling between
synthesis and analysis. The 96/384 system can be operated stand alone or by a robot system.
PODIUM ABSTRACTS