Today
the pharmaceutical discovery lab faces the challenges of:
1) reducing drug development time
2) speeding up identification of new and validated drug targets
3) developing high-quality information early in the discovery process
Proteomics, informatics, and protein
microarrays potentially meet all three of these needs; yet integration
is critical for maximizing their potential for success. Complete
discovery research is a team effort including basic biological
researchers, application researchers, bioinformaticists, database
developers, chemists, and engineers (software, material, and
microfluidic). This program incorporates each discipline into a
comprehensive unit to produce profitable results.
Scientific Advisors:
Dr. Dolores J. Cahill, Max-Planck-Institute of Molecular Genetics
Dr. Ian Humphery-Smith, University of Utrecht
Dr. Michael Taussig, The Babraham Institute
Dr. Markus Templin,
University of Tübingen
Dr. Mathias Uhlén, Royal Institute of Technology and Affibody AB
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Keynote Presentations
Searching for Therapeutic Strategies from Genetic Analysis and
Primary Disease Mechanisms
Prof. John Todd, Professor of Medical Genetics and Director of JDRF/WT
Diabetes & Inflammation Laboratory, University of Cambridge
The Proteome:
How Do We Find Any More
Pharmacologically Active Proteins?
Dr. Massimo de Francesco, Global Head of Scientific
Computing, Serono Pharmaceutical Research Institute
Dr. Jan-Anders Karlsson, Executive Vice President, Pharma Research,
Bayer AG Leverkusen
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Additional Speakers
Dr. Peter J. Boogaard, Applera Corporation
Dr. Jennifer Brockman, HTS Biosystems, Inc.
Dr. Dolores J. Cahill, Max-Planck-Institute of Molecular Genetics
Dr. Hauke Clausen-Schaumann, nanotype GmbH
Dr. Emmanuel Delamarche, IBM Zurich Research Laboratory
Dr. Christoph Eckerskorn, Tecan Munich GmbH
Dr. Petra Söhnlein, QIAGEN GmbH
Dr. Mathias Goeschl, LION bioscience AG
Dr. José Luis Pérez Gracia, Eli Lilly & Co., Inc.
Dr. Christoph Hüls, Protagen AG
Dr. Ismail Moarefi, SiREEN AG
Dr. Keith Rose, GeneProt, Inc.
Dr. Bruce Seligmann, High Throughput
Genomics
Dr. Arne Skerra, PIERIS Proteolab AG
Dr. Ulf Skoglund, Karolinska Institute and Sidec Technologies AB
Dr. Serhiy Souchelnytskyi, Ludwig Institute for Cancer Research
Dr. Giulio Superti-Furga, Cellzome AG
Dr. Michael Taussig, The Babraham Institute
Dr. Markus Templin, University of Tübingen
Dr. Peter Uetz, Forschungszentrum Karlsruhe
Dr. Mathias Uhlén, Royal Institute of Technology and Affibody AB
Protein Structure and Interactions
Two-Hybrid Yeast System
3-D Conformation with Electron Tomography
SiREENscreen and SiREENvalid
Anticalins
Proteome Profiling
Industrial-Scale Proteomics
Functional Proteomics of TGFß Signaling
Global Genomics and Protein Information
Embedding Proteomics Discovery into a Scalable Data Integration
Overcoming Common Bottlenecks
A Human Protein Resource Initiative
Protein Arrays
Protein Microarray Technology
Recent Developments in Array Technology
Patterning Proteins Using Soft Lithography
Plasmon Resonance Biosensor for Label-Free Sensing
Differential Protein Expression Profiling
Ligand binders
Double Chip Format for True Multiplexing
Drug Discovery Applications
Identification of Drug Targets for CNS Disorders
Lead Compounds via Integrated Proteomics Approaches
Exploiting Tractable Drug and Target Space
Finding Drug Targets Using Functional Genomics
Phenotype Selection Studies in Cancer Research
Program
Wednesday, April 23
16.00-18.00 Early Registration
Thursday, April 24
7.00 Registration, Poster and Exhibit Set-up,
and Light Continental Breakfast
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Keynote Presentations
8.30 Chairperson's Opening Remarks
Dr. Mathias Uhlén, Department of Biotechnology, Royal Institute of Technology
(KTH); and Affibody AB
8.40 Searching for Therapeutic Strategies from
Genetic Analysis and Primary Disease Mechanisms
Prof. John Todd, Professor of Medical Genetics and Director of JDRF/WT
Diabetes & Inflammation Laboratory, University of Cambridge
The interrogation of the allelic variation of the genome responsible for
common human disease and for experimental models of these disorders is in its
infancy. The search for disease risk causing variants is now aided by advances
in genome sequence determination, genotyping methods, and the acquisition of
appropriately large study sample sizes. Identification of candidate causal
variants directs functional studies that lead to insights into the causal
mechanisms of disease, thereby avoiding research effort into pathways that are
an effect of the disease process rather than a primary etiological factor.
9.15 The Proteome: How Do We Find Any More
Pharmacologically Active Proteins
Dr. Massimo de Francesco, Global Head of
Scientific Computing, Serono Pharmaceutical Research Institute
One of the key hopes of the genome age is that the deeper understanding of the
human genome would lead to a wave of new therapeutics. As one of the world's
leading biotechnology companies, Serono is searching for the next generation
of protein products in its disease areas, be they cytokines, growth factors
and hormones, or engineered proteins that can block the action of such
cytokines. Our project to understand the secreted protein universe will be
discussed—from novel bioinformatics that is still identifying the sequence
of proteins, through to disease-based technologies for understanding the
therapeutic applications of proteins.
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9.50 Opening of Poster and Exhibit Hall,
Refreshment Break
Protein Structure and Interactions
10.30 Chairperson's Remarks
Dr. Markus Templin, Head of Microarray Technology,
Natural and Medical Science Institute (NMI), University of Tübingen
10.35 Two-Hybrid System in Basic Research and
Drug Discovery
Dr. Peter Uetz, Group Leader, Institute of Genetics (ITG), Forschungszentrum
Karlsruhe
The two-hybrid system is a powerful method for detecting protein-protein
interactions. Various flavors of the two-hybrid system such as random and
directed approaches differ in the number of false positives and false
negatives they produce. Some applications of various two-hybrid systems for
drug discovery will be described.
11.05 Visualizing the 3-D Conformation of
Individual Proteins with Sidec™ Electron Tomography
Dr. Ulf Skoglund, Professor, Department of Cell and Molecular Biology,
Karolinska Institute; and Chief Scientific Officer, Sidec Technologies AB
Today it is possible to determine the 3-D structure of proteins in a
biological specimen, e.g., a protein solution or a tissue section, using
low-dose electron beam intensity and recordings from a large number of view
angles in a transmission electron microscope (TEM). This technology is termed
electron tomography. Refinement software developed at Sidec Technologies
allows the 3-D reconstruction, or tomogram, to be generated at around 2 nm
resolution for proteins in buffer solution and between 2-3 nm resolution for
proteins in situ, e.g., in their membrane setting. Thus, individual protein
molecules can be scrutinized in a specific buffer for their conformational
flexibility or their tendency to deviate from a perhaps known X-ray
crystallographic structure. The stoichiometry and flexibility of
multicomponent structures can be analyzed in buffer as well as in situ. As of
today, it takes about one day of active work to go from the practical steps of
specimen data collection in the TEM until the tomogram can be seen rotating on
a computer screen. Here we present approved examples from customer projects to
illustrate how Sidec™ Electron Tomography (SET) has improved the 3-D
characterization of proteins within drug discovery.
11.35 SiREENscreen and SiREENvalid: Integrated
Technologies for the Development of Highly Specific Small Molecule Drugs
Dr. Ismail Moarefi, Chief Scientific Officer, SiREEN AG
The ultimate goal in the design of small molecule inhibitors for therapeutic
purposes is a compound that only affects the disease causing target proteins
in an organism. Molecules that are structurally related to the target proteins
do, however, have a high likelihood of cross-reacting with the inhibitor,
severely increasing the likelihood of unwanted and adverse side effects that
are not caused by the inhibition of the target molecules and could be avoided
by developing more selective compounds. Current hit profiling and target
validation methods can address the problem of specificity in target compound
interaction only partially, leading to a large number of poorly characterized
compounds entering clinical trials that will fail later on due to unwanted
side effects. SiREENscreen and SiREENvalid are technologies that have been
developed with the aim of extensively characterizing the selectivity profile
of target/compound interactions for reliable compound development and
chemogenomic target validation.
12.05 Anticalins: Small Robust Target-binding
Proteins Derived from the Lipocalin Scaffold
Dr. Arne Skerra, Vice Chairman and Co-founder, PIERIS Proteolab AG
Anticalins are derived from natural lipocalin proteins via site-directed
random mutagenesis and phage display selection against prescribed haptens or
antigens. Their molecular architecture comprises a circular eight-stranded
antiparallel beta-sheet. At one end four loops that connect each pair of
neighboring beta-strands form the entrance to the ligand-binding site. Whereas
the beta-barrel structure is highly conserved, the loop region is
hypervariable and can be reshaped for molecular recognition. While the first
anticalins have been selected against small ligands, suitable libraries have
recently been constructed in order to create anticalins with high affinities
and specificities toward protein targets. Anticalins offer advantageous
properties for substituting conventional antibodies in several areas, for
example as bioanalytical reagents or even in medical therapy.
12.35 Lunch (on your own)
Proteome Profiling
14.00 Chairperson's Remarks
Dr. Dolores J. Cahill, Group Leader, Protein Technologies Group,
Max-Planck-Institute of Molecular Genetics
14.05 Industrial-Scale Proteomics of Human
Blood Plasma
Dr. Keith Rose, Chief Scientific Officer, GeneProt, Inc.
GeneProt has analyzed four pools of 2.5 liters of human blood plasma in a
study of coronary artery disease. Proteins with Mr < 25'000 were separated
by chromatographic techniques, while proteins with Mr > 25'000 were
separated by chromatographic techniques followed by gel electrophoresis. Many
millions of mass spectra were obtained and processed. Results have been
incorporated into a database and interesting proteins synthesized for
bioassay.
14.35 Functional Proteomics of TGFß
Signaling: Will New Targets Become New Drugs?
Dr. Serhiy Souchelnytskyi, Assistant Member, Ludwig Institute for Cancer
Research
Transforming growth factor-ß
(TGFß) is a potent regulator of
cell proliferation, differentiation, migration, and apoptosis. We use
two-dimensional gel electrophoresis and mass spectrometry to identify new
targets of TGFß
signaling and new proteins interacting with TGFß
signaling components, e.g., receptors and Smads. We analyze pattern of protein
expression by silver staining and by labeling cells with 35S or 32P. We
identified more than 30 targets of TGFßand unveiled new regulatory
pathways in TGFß
signaling. Possible use of the identified targets for
drug discovery will be discussed.
15.05 Enabling the Next Information Technology
of Molecular Discovery
Dr. Peter J. Boogaard, Senior Manager, Applied Biosystems, and Marketing
Intelligence Manager Europe, Applera Corporation
Progress in our functional understanding of human biology is possible as never
before. But this understanding, and new opportunities in drug discovery and
diagnostics, can only be realized if we can build on the information from the
genome and leverage it at a practical level in the laboratory. The greatest
challenge is to allow scientists to use global genomics and protein
information in a local setting to allow discovery by a scientist, with a
hypothesis, conducting experiments. This presentation will focus on the ways
the Applera Corporation is providing technology and information solutions that
help scientists understand and use the power of biology and information
technology. This approach includes providing validated content of databases,
and validated assays for that content, and integrating on-line data in
experiments as well as integrating software and instruments through a
professional services group to bring tailored informatics solutions for
managing and automating laboratories.
15.35 Poster and Exhibit Viewing, Refreshment
Break
16.15 The LION TargetEngine™: Embedding
Proteomics Discovery into a Scalable Data Integration Framework
Dr. Mathias Goeschl, Director, Proteomics, LION bioscience AG
Based on the LION DiscoveryCenter™ integration platform, LION presents a
modular architecture to support scalable solutions in the area of proteomics,
embedded in fundamental data provided by other disciplines, e.g., genomics and
transcriptomics. A demonstration of the system is given on the basis of
cholesterol homeostasis, including extensive information about cholesterol
metabolism and the genetic and post-translational regulation of key enzymes.
Basically, the integration of cholesterol-related pathway information from
different data sources is used as a framework, whereas systematic analysis of
scientific literature is used to extend this knowledge. The results indicate
that there is no functional separation between biochemical, signaling, and
gene regulatory pathways. This enables us to illustrate the functional link
between metabolome, genome, and proteome, e.g., combined feedback regulation
by biochemical and genetic mechanisms. Through further data integration, the
relevant targets are directly linked to important auxiliary information, e.g.,
protein structures, gene expression, and genomic organization.
16.45 Automated Protein Analyses: Overcoming
Common Bottlenecks
Dr. Christoph Eckerskorn, Chief Scientific Officer, Tecan Munich GmbH
Traditional manual techniques lack one or more of the following basic
requirements for successful proteomic analyses: fractionation (i.e., the
reduction of complexity), sensitivity (i.e., the detection of unknown, low
abundant proteins), reproducibility (i.e., the generation of scientifically
significant results), and throughput (i.e., the generation of large amounts of
valuable data in a short period of time). To address these critical needs,
TECAN has developed the automated ProTeam™ platform consisting of different
modules: a Free-Flow Electrophoresis System (a (semi) preparative,
charge-based, liquid separation technology for the fractionation of cells,
cell organelles, and complex protein mixtures); a fully automated 2D-PAGE
System (including IEF, gel casting, SDS-PAGE, staining); and a Protein
Processing System (a spot picking device followed by an in-gel digester and an
interface to mass spectrometers). The modules can be flexibly combined (e.g.,
a direct combination of free-flow electrophoresis with LC-MS), which allows
researchers to set up a customized platform for all kinds of proteomics
applications (e.g., drug discovery, drug validation, screening, etc.).
17.15 A Human Proteome Resource Initiative
Dr. Mathias Uhlén
A systematic approach to convert genomics data into biological knowledge based
on protein profiling has been initiated. The strategy relies on a
high-throughput method for the recombinant production of non-homologous
regions of the proteome selected by whole genome bioinformatics. Such protein
fragments are individually used to generate and enrich mono-specific
antibodies for systematic analysis of protein objective of this affinity
proteomics strategy to produce a proteome atlas, describing distribution and
expression of proteins in normal tissues as well as in common cancers and
other forms of diseased tissues.
17.45 Networking Reception
19.00 Close of Day One
Friday, April 25
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7.30-8.15 Breakfast
Workshop:
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Protein Atlas of the Human Genome:
Integrating Genomics and Proteomics
Presented by: Dr. Michael Taussig, Confirmant Ltd
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Protein Arrays
8.30 Chairperson's Remarks
Dr. Michael Taussig, Chairman, European Science
Foundation Programme
in Functional Genomics, and Head, Technical Research
Group, The Babraham Institute
8.35 Protein Microarray Technology
Dr. Markus Templin
DNA chips have become an established technology. Their application for
generating transcriptional profiles of genes at a genomewide level has led to
a wealth of new insights. Within the last few years, methods based on
microarray technology have been adapted to the analysis of proteins, and novel
applications have emerged. Protein microarrays offer the fascinating
possibility to study protein interactions in a massively parallel fashion,
including protein-protein and enzyme-substrate interactions. The use of
protein microarrays in diagnostic applications has led to the establishment of
novel analytical systems. A rapid and low-cost analysis of a multitude of
analytes from minute amounts of sample is possible and makes the use of
protein microarrays interesting for diagnostic purposes. Data of protein
microarray-based assays that are currently performed at the NMI will be
presented and discussed.
9.05 Proteins Arrays: Recent Developments
Dr. Dolores J. Cahill
Recent applications of protein arrays, including profiling the antibody
repertoire of autoimmune patients, and the determination of the specificity or
cross-reactivity of antibodies will be described.
9.35 Patterning Proteins on Surfaces Using Soft
Lithography Techniques
Dr. Emmanuel Delamarche, Research Staff Member, IBM Zurich Research Laboratory
Patterning proteins on surfaces opens the route to miniaturizing bioassays
with the attendant benefits of economizing reagents, and detecting analytes in
parallel with minimal time and high-quality signals. We have developed
methods, based on soft lithography, to pattern proteins—down to the level of
a single protein molecule—on surfaces for immunoassays. Soft lithography
refers to a set of techniques utilizing a stamp to pattern surfaces. With
"microcontact printing," it becomes simple to ink proteins onto a
stamp and to transfer them on a variety of substrates with submicrometer
accuracy. For example, one thousand antibody molecules can be printed within a
1 µm2 region of a silicon surface and used for immunoassay experiments. In
"affinity contact printing," stamps are tailored to have affinity
for specific proteins from an ink. An alternative to printing is to use a
patterned elastomer to define microfluidic networks on a surface. These
microfluidic networks are free of external pumping elements and are ideal to
conduct surface, sandwich immunoassays in a combinatorial fashion, on a planar
surface, with high resolution and contrast, using submicroliter quantities of
samples and reagents, and on a time scale of a few minutes.
10.05 Poster and Exhibit Viewing, Refreshment
Break
10.30 A Surface Plasmon Resonance Biosensor
for Label-Free, Array-Based Sensing in Proteomics Research
Dr. Jennifer Brockman, Manager of Surface Chemistry, HTS Biosystems,
Inc.
HTS Biosystems has developed a novel, high-information-content,
high-throughput
biosensing platform useful in the study of a broad range of biomolecular
interac-tions
(e.g., antibody-antigen, protein-protein, protein-nucleic acid, etc.). The
label-free,
surface plasmon resonance (SPR) technology employed allows the user to
simultaneously monitor the kinetics of hundreds of binding events on a single
array. The proprietary, grating-based coupling scheme allows for the cost-effec-tive
production of disposable plastic biosensors crucial for high-throughput
screen-ing
applications. In addition, a flexible optical design allows for a massively
par-allel
detection scheme that positions the SPR platform as the lowest cost, highest
throughput, and most flexible label-free detection platform available.
Presentation
topics will include an introduction to the grating-coupled SPR technology,
specifics
of the SPR platform, surface attachment chemistries, array preparation, and
data
analysis. As an example, the binding of FITC-labeled targets to arrays of
surface-bound
anti-FITC monoclonal antibodies will be discussed.
11.00 Advances
in Multiplex Protein Suspension Arrays
Dr. Petra Söhnlein, Senior Scientist, R&D Protein
Expression & Proteomics, QIAGEN GmbH
Given the complexity and interconnectedness of the proteome, analysis
methods that provide a complete overview of complete enzyme families (e.g.,
chemokines and cytokines) or cell-signaling pathways (e.g., kinase cascades)
are significantly more valuable than single-enzyme assays. The QIAGEN
LiquiChip System uses bead-based xMAP technology to enable the simultaneous
quantification of up to 100 different analytes in a single small-volume
sample, providing high-content assay data for life-science research and drug
discovery. Adapting 6xHis-tag technology to the xMAP assay platform enables
purification, immobilization, and detection of biologically active proteins
using a single chemistry; increasing standardization and saving time during
assay setup and development. In addition, the oriented immobilization provided
by the 6xHis tag increases signal intensity and assay sensitivity and
reproducibility, compared with random immobilization used in many array
platforms. To increase assay throughput and reproducibility, the entire
protein purification and assay process can be automated. The high Z'-factor
values obtained in an exemplary assay reflect the robustness of the LiquiChip
System and its suitability for the types of assay carried out in the drug
discovery process.
11.30 Ligand binders and Protein Arrays
Dr. Michael Taussig
In order to make use of the genome information to identify proteins, whether
on arrays or by other means, we require a comprehensive collection of "ligand
binders" against the proteome. Ligand binders include classical
antibodies and their recombinant single-chain and single-domain forms, as well
as novel protein scaffolds and nucleic acid aptamers. Ligand binders will be
used in protein capture microarrays to monitor protein expression levels, in
tissue arrays to demonstrate protein localization, and as reagents for protein
isolation by affinity methods. A critical issue when using large numbers of
ligand binders simultaneously is specificity of binding. Cross-reactivity in
highly multiplexed assays will lead to potentially disastrous false-positives
and is now seen as the number one problem for capture arrays. In this
presentation, strategies for making a resource collection of ligand binders
against the proteome and methods for optimizing the specificity and
sensitivities of protein arrays will be discussed
12.00 A New Double Chip Format for True
Multiplexing of Protein Assays
Dr. Hauke Clausen-Schaumann, Head of Science, nanotype GmbH
Protein assays provide direct access to biologically and pharmacologically
relevant information. To obtain a maximum of information from small amounts of
complex biological samples, there is a growing need for highly multiplexed
protein assays. In single marker assays, pairs of capture and detection
antibodies, with the capture antibodies bound to a solid support and the
detection antibodies carrying specific labels, are generally used to increase
the specificity and precision of the assay. However, when used in a
multiplexed assay, both capture and detection antibodies are plagued by
cross-reactions and nonspecific binding. This results in many false positives
and a background signal, which grows faster than the number of spots on a
chip, or the number of different beads in a bead-based assay. Here we present
a new double chip format, where the sample solution is applied to a primary
array of capture antibodies and the labeled detection antibodies are connected
to a second chip surface via molecular force sensors. Upon binding of the
analyte molecules, the two surfaces are brought into contact to allow for
binding of the detection antibodies. The two surfaces are then separated again
and, only if a detection antibody could form a specific bond to its
corresponding antigen, the force sensor yields and the labeled detection
antibody is transferred to the primary chip surface, where it can be detected
using standard readout devices, e.g., fluorescence scanners. This new format
allows for true multiplexing of protein assays, without costly and
time-consuming optimization of antibodies, because here cross-reactions and
nonspecific binding do not lead to false positive results and the background
signal is independent of the number of spots on the chip.
12:30 Lunch (on your own) (sponsorship
opportunities available)
Drug Discovery Applications
13.45 Chairperson's Remarks
Dr. Giulio Superti-Furga, Vice President, Biology, Cellzome AG
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13.50 Keynote Address: Drug Discovery in the
Post-genomic Era-Delivering High Quality
Development Candidates
Dr. Jan-Anders Karlsson, Executive Vice President, Pharma Research,
Bayer AG, Leverkusen
The wealth of genomic data made available to researchers in recent years, has
brought with it the promise of a rapid unravelling of molecular disease
mecha-nisms and an expectation of the discovery of novel and more effective
medi-cines. A variety of DNA based and other high throughput
technologies are wide-ly used for this purpose in discovery research.
Additional protein based methods and strategies are now required for both a
rapid and thorough understanding of disease processes. The identification and
validation of disease targets at the molecular level, combined with chemical
research as well as a number of other relevant drug discovery technologies,
will enable the identification of high qual-ity "low molecular
weight"- and protein-based- drugs for diseases with high unmet medical
need.
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14.30 Bridging the Gap Between Genomics and
Proteomics
Dr. Bruce Seligmann, President and Chief
Executive Officer, High Throughput Genomics
Studying the transcriptome has been a major hurdle for drug discovery,
until now, and has been ignored due to lack of appropriate commercially
available tools. Researchers have jumped from studying the genome to the
proteome, ignoring RNA, because they could not accurately study it. Yet, there
are many drugs and compounds that work at the level of the transcriptome
(e.g., hormones, vitamins and steroids). In the coming year, scientists will
begin to recognize that they can get better information about potential new
drugs and consequently compress the drug discovery and development process, by
using new technologies to perform drug discovery at the gene expression level.
15.00 New Lead Compounds via Smart Integrated
Proteomics Approaches
Dr. Christoph Hüls, President and Chief Executive Officer, Protagen AG
The post-genomic era left pharmaceutical R&D with a huge number of
possible disease-related targets, their respective validation in accepted
pharmaceutical in vitro and in vivo models, and the task to
design and to develop lead candidates and new chemical entities (NCEs). Until
today, proteomics technologies proved to be decisive for target discovery and
validation only. Protagen shows that the strategic application of its
proprietary integrated proteomics technology (IPT™) platform allows the
straightforward design of small molecule lead compounds with significant
biological activity. The Protagen strategy is based on the identification of
regulatory networks of cellular proteins affected by already marketed drugs in
diseased and normal states. The extraction of knowledge from these proteomics
studies and its correlation with the basics in cell biology, biochemistry, and
pharmacology can be applied to the design of small molecule drugs. In this
study, an anti-proliferative and anti-inflammatory drug was used to identify a
set of proteins all belonging to the major cellulary energy generating
machinery. The comparison of drug structures and natural substrates as well as
effectors of these proteins gave guidance for the synthesis of P@G1011. The
new lead candidate has been tested in vitro and in animal models and
showed efficacy in different cell lines and in a rat cancer model. These data
strongly demonstrate the potential of smart designed proteomic studies in
delivering superior quality of targets and lead compounds and in speeding up
the pharmaceutical R&D process.
15.30 Poster and Exhibit Viewing, Refreshment
Break
16.00 Drug Proteomics: Exploiting Tractable
Drug and Target Space
Dr. Giulio Superti-Furga
Cellzome AG is an emerging biopharmaceutical company using known drug and
target space to exploit the proteome in an efficient and focused approach.
Previously unrecognized connections between proteins and protein complexes,
drugs, and biological processes are identified with proprietary proteomics
technologies. Using this unique perspective, Cellzome has the ability to
select druggable targets, choose lead molecules with key features, and reject
targets with safety concerns. This can be accomplished very early in the drug
discovery process, circumventing future safety concerns and streamlining the
process to focus only on the most promising compounds.
16.30 To Be
Announced
17.00 Extreme Phenotype Selection Studies in
the Identification of Relevant Genotypes in Cancer Research
Dr. José Luis Pérez Gracia, Clinical Research Physician, European Medical
Department, Eli Lilly & Co., Inc.
The investigation of genetic alterations that are potentially related to the
prognosis of cancer patients has become a frequently used strategy in recent
years, but many times it has led to conflicting results. In contrast, the
identification and the study of subjects or families with very characteristic
phenotypes have yielded outstanding results in the identification of the
genetic characteristics underlying such phenotypes. While on most occasions
the individuals selected for these types of studies were characterized by a
negative phenotype—for example, an increased risk to develop a determined
disease—a few studies have been directed towards individuals with phenotypes
of unusual good prognosis—i.e., those presenting a decreased risk of
developing determined diseases despite an important exposure to well-known
risk factors. Therefore, it seems logical to further develop this strategy as
a valid methodology for the study of other diseases such as cancer. The study
of individuals with phenotypes of extremely good prognosis, such as long-term
survivors of theoretically incurable tumors or of subjects that seem to be
protected against certain neoplastic disorders despite possessing a markedly
increased risk to develop them, could unveil the genetic alterations that
explain such characteristic phenotypes and could provide potentially useful
therapeutic targets against this disease.
Close of Conference
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|
Linking Phenotype to Genotype and Proteins to Profits concurrent
conferences will provide an excellent venue for companies wishing to
network with scientists from the biotechnology and pharmaceutical
industries involved in the correlation of phenotype to genotype and/or
scientists involved in the technical developments or applications in the
fields of Protein and Peptide Arrays and Proteomics. Cambridge
Healthtech Institute offers an array of sponsorship packages for you to
most successfully reach this select audience. Make a lasting impression
as a leader in these areas by taking advantage of these marketing tools.
All packages can include an exhibit space or an exhibit space can be
purchased alone. |
HOTEL INFORMATION
Hilton Munich Park
Am Tucherpark 7
D-80538 Munich, Germany
T: 49-89-3845-0, F: 49-89-3845-2588
Room Rates: Euro 155/S, Euro 175/D
Cut-off Date: April 1, 2003
Please call the hotel directly to make your room reservation. Identify
yourself as a Cambridge Healthtech Institute conference attendee to
receive the reduced room rate. Reservations made after the cut-off date
or after the group room block has been filled (whichever comes first)
will be accepted on a space-and-rate-availability basis. Rooms are
limited, so please book early.
CALL FOR POSTERS
Cambridge Healthtech Institute encourages attendees to gain further
exposure by presenting their work in the poster sessions. Please fill
out the registration form, with the poster title and primary author. To
ensure inclusion in the conference CD, a one-page summary must be
submitted and registration must be paid in full by March 21, 2003. Click
here for poster instructions
For additional information, please
contact Deborah Brooks at 781-972-5412 or dbrooks@healthtech.com
OR Angela Parsons at 781-972-5467 or aparsons@healthtech.com. |
