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Immediately prior to CHI's Third Annual Recombinant Antibodies conference.

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Sponsoring Publications:
Drug Discovery and Development
Human Antibodies
Immunotherapy Weekly
The Scientist
Protein Science

Phage display is a fundamental tool in protein engineering. The directed evolution of proteins using display methods can be engineered for specific properties and selectivity. This year's meeting will delve into the new methods involved in protein detection, amplification, and directed evolution. This is essential to the proteomics effort aimed at identifying, mapping, and understanding all human proteins in a comprehensive manner. A variety of display approaches are employed for the engineering of optimized human antibodies, as well as protein ligands, for such diverse applications as protein arrays, separations, and drug development. The use of phage display in screening for novel high-affinity ligands and their receptors has been crucial in functional genomics and proteomics. Display methods will make it possible to target essential components and pathways within many different diseases, including cancer, AIDS, cardiovascular disease, and autoimmune disorders.

SCIENTIFIC ADVISORY BOARD
Dr. Andrew Bradbury, Los Alamos National Laboratory
Dr. Hennie R. Hoogenboom, Dyax SA and University of Liège
Dr. Renata Pasqualini, University of Texas M.D. Anderson Cancer Center
Dr. Richard Wagner, Phylos Inc.
Dr. Gregory A. Weiss, University of California, Irvine
Dr. K. Dane Wittrup, Massachusetts Institute of Technology

SPEAKERS
Dr. David J. Austin, Yale University
Dr. Carlos F. Barbas III, The Scripps Research Institute
Dr. Joel Belasco, New York University School of Medicine
Dr. Andrew Bradbury, Los Alamos National Laboratory
Dr. Stephen P. Hale, Phylos Inc.
Dr. Paul T. Hamilton, Karo Bio USA, Inc.
Dr. Tara Heitner, BioTrove Inc.
Dr. Simon E. Hufton, Dyax SA
Dr. Brian Kay, Argonne National Laboratory
Dr. Anthony A. Kossiakoff, University of Chicago
Dr. Robert Charles Ladner, Dyax Corp.
Dr. Henry B. Lowman, Genentech, Inc.
Dr. Ed Madison, Torrey Pines Institute for Molecular Studies and Corvas International
Dr. Barbara Morris, Novagen, Inc.
Dr. Richard Roberts, California Institute of Technology
Dr. Michael Roguska, Abbott Bioresearch Center
Dr. Jamie K. Scott, Simon Fraser University
Dr. Jackie Sharon, Boston University School of Medicine
Dr. Glenn F. Short III, Massachusetts General Hospital
Prof. Arne Skerra, Technische Universität München
Dr. John Smit, University of British Columbia
Dr. Veerle Somers, Maastricht University and Dyax SA
Dr. Toru Tsuji, Mitsubishi Kagaku Institute Of Life Sciences
Dr. Gregory A. Weiss, University of California, Irvine
Dr. James A. Wells, Sunesis Pharmaceuticals
Dr. K. Dane Wittrup, Massachusetts Institute of Technology

 

PHAGE-BASED SMALL MOLECULE DISCOVERY
Keynote Presentation
Site-Directed Drug Discovery
Dr. James A. Wells, Sunesis Pharmaceuticals
Selection of cDNA Clones from Display Libraries
Identifying Low-Affinity Interactions with cDNA Phage Display
Lipocalins as a Scaffold for the Recognition of Target Molecules
Peptides from Phage Display Libraries as Tools for Drug Discovery

DISPLAY TECHNOLOGIES
Mapping Protein-Protein Interactions with Combinatorial Peptide Libraries
Discovery and Optimization of Peptide Ligands Using mRNA Display
Yeast Display for Affinity Maturation of Human Fab Antibodies
Peptide Phage Display for Vaccine Development on Anti-HIV Antibody
Exploiting the Bacterium Caulobacter to Display Libraries of Peptides
DNA Microarrays to Deconvolute the Results of mRNA-Display

DIRECTED PROTEIN EVOLUTION TECHNIQUES
Protein Engineering by Yeast Surface Display
Shotgun Scanning
Selecting Ultrahigh-Affinity Binders Routinely Using mRNA Display
Construction of Combinatorial Protein Libraries
T7 Phage Display to Clone RNA-Binding Proteins
Applying Phage Display to Functional Genomics

GENERATION AND SELECTION OF LIGANDS AND ANTIBODIES
Zinc Finger Proteins and the Control of Endogenous Genes
Antagonists of IgE from Phage Display
Elucidating Substrates of Human Fibrinolytic Serine Proteases
Novel Protein Engineering Tool Combining Chemical and Biological Approaches
Profiling the Cancer Immunome Using Phage cDNA Display
Polyclonal Antibody Libraries for Cancer and Infectious Diseases
Antibody and Protein Arrays

SUNDAY, APRIL 21

5:00-7:00pm Early Registration and Poster and Exhibit Setup

 

MONDAY, APRIL 22

7:00am Registration, Poster and Exhibit Viewing, and Light Continental Breakfast

 

PHAGE-BASED SMALL MOLECULE DISCOVERY

8:30 Chairperson's Opening Remarks
Dr. Robert Charles Ladner, Senior Vice President and Chief Scientific Officer, Dyax Corp.

8:40 KEYNOTE PRESENTATION
SITE-DIRECTED DRUG DISCOVERY
Dr. James A. Wells, President and Chief Scientific Officer, Sunesis Pharmaceuticals, Inc.
The Means by which proteins recognize other proteins and small molecules is fundamental to protein and small molecule design. We have been developing a novel drug discovery technology we call tethering. Tethering is an approach to find weak drug fragments (MW~200 Da) to nucleate the drug discovery process. A native or engineered thiol in a protein is allowed to react reversibly under thiol exchange conditions with a small library of disulfide-containing small molecules at concentrations that are typical for drug screening. The thiol-captured ligands, which are identified by mass spectroscopy, represent the most stable complexes even though in the absence of the covalent tether the most stable ligand may bind very weakly (Ki ~ 1mM), compounds that would be undetectable by High Through-put Screening (HTS). Moreover, the method provides binding stoichiometry and site location for the tethered compounds, data which are not immediately available by HTS. These nucleating fragments can be affinity optimized using a combination of structural analysis and medicinal chemistry. Tethering was applied to generate potent inhibitors for two enzymes and a protein-protein target, which have resisted drug discovery by standard HTS.

9:15 Selection of cDNA Clones from Display Libraries Constructed in Bacteriophage T7
Dr. Barbara Morris, Senior Scientist, Product Applications, Novagen, Inc.
The genome of the lytic phage T7 has been engineered to accept inserts as large as 3.6 kb and display the products as C-terminal fusions to the major capsid protein. Use of a lytic phage as a display platform eliminates the requirement for a secretory pathway for release of mature phage from infected cells. The C-terminal fusions impose no constraints on reading frame or the inclusion of a stop codon in the cDNA insert. Among the applications to be described are determination of antibody specificity, isolation of binding domains, and selection of phage with affinity for an animal virus.

9:45 Elution Is the Solution: Identifying Low-Affinity Interactions with cDNA Phage Display
Dr. David J. Austin, Associate Professor, Department of Chemistry, Yale University
Since its first introduction with natural products, the use of cDNA phage display for the discovery of cellular protein targets has grown to include signaling peptides, RNA, and DNA probes. Under standard selection conditions, protein targets with the highest affinity for the probe are isolated, often at the expense of lower affinity clones. Recent developments in screening technology, namely elution conditions, have facilitated the isolation of lower affinity targets, and the use of low affinity probes, with increased success. These developments, along with the benefits and drawbacks of this technique, will be discussed.

10:15 Poster and Exhibit Viewing, Refreshment Break

11:00 Anticalins: Lipocalins as a Scaffold for the Recognition of Small and Large Target Molecules
Prof. Arne Skerra, Lehrstuhl für Biologische Chemie, Technische Universität München
The molecular architecture of lipocalin proteins comprises a circularly closed eight-stranded beta-sheet that winds around a central axis. At one end this beta-barrel is open to the solvent and four loops connecting each pair of neighboring antiparallel beta-strands form the entrance to the ligand-binding site. While the beta-barrel structure is highly conserved, the loops vary considerably in sequence, length, and conformation among the individual family members, thus explaining their differing ligand specificities. This feature prompted us to reshape the lipocalin-binding site, using random mutagenesis and phagemid selection, in order to create compact and robust receptor proteins, so-called anticalins, that can tightly complex prescribed small compounds (like fluorescein and digoxigenin) and even protein targets.

11:30 Peptides from Phage Display Libraries as Tools for Drug Discovery
Dr. Paul T. Hamilton, Director of Research, Karo Bio USA, Inc.
Using selectively biased phage display peptide libraries, we have isolated high-affinity peptide probes directed to biologically relevant sites on target proteins. These peptides can be used as tools for proteomic analysis and in drug discovery. At Karo Bio, we have used peptides to format HTS-compatible assays for targets that are difficult to screen by traditional HTS methods and identified active compounds. We have expressed target-directed peptides inside cells and shown that they affect biological function as a method of target validation. Karo Bio has developed assays for G-protein-coupled receptors using peptides that detect activation of a G-protein. In addition, we have identified protein conformation-dependent peptides for nuclear receptors that can be used in an in vitro assay to predict the biological response produced by compounds.

12:00 Panel Discussion

12:30 Lunch (on your own)

 

DISPLAY TECHNOLOGIES

1:45 Chairperson's Remarks
Dr. K. Dane Wittrup, J.R. Mares Professor, Chemical Engineering and Bioengineering, Massachusetts Institute of Technology

1:50 Mapping Protein-Protein Interactions with Combinatorial Peptide Libraries
Dr. Brian Kay, Senior Biochemist and Group Leader, Biosciences Division, Argonne National Laboratory
A fruitful approach for mapping protein-protein interactions is to isolate peptide ligands from a phage-displayed combinatorial peptide library to a target protein and then identify candidate interacting proteins in a sequenced genome by computer analysis. We will present several examples of this method applied to dissecting molecular interactions in the protein machinery involved in receptor-mediated endocytosis.

2:20 Trillions of Molecules, So Little Time: Discovery and Optimization of Peptide Ligands using mRNA Display
Dr. Richard W. Roberts, Assistant Professor of Chemistry, Division of Chemistry and Chemical Engineering, California Institute of Technology
mRNA display provides a means to generate and sieve peptide and protein libraries with more than one trillion members, entirely in vitro. We have recently applied this approach to isolate high affinity RNA-binding peptides. This work has resulted in molecules that bind a common RNA structural element, the GNRA tetraloop. Our recent efforts to extend and generalize this approach to more complicated RNA targets will be presented.

2:50 Yeast Display for Affinity Maturation of Human Fab Antibodies
Dr. Simon E. Hufton, Director of Research, Dyax SA
The rapid and efficient affinity maturation of biomolecules is a critical component of the drug development pipeline. Selection of yeast-displayed repertoires by fluorescent-activated cell sorting has proven an effective method for the affinity maturation of scFv antibodies. We present the affinity maturation of human Fab antibodies by similar selection of yeast-displayed repertoires. Furthermore, the use of the yeast mating life cycle to generate combinatorial diversity will be presented, and application to both affinity maturation and the generation of large naïve antibody repertoires will be discussed.

3:20 Poster and Exhibit Viewing, Refreshment Break

4:00 Peptide Ligands for Neutralizing Antibodies Against HIV-1
Dr. Jamie K. Scott, Associate Professor, Department of Molecular Biology and Biochemistry, Simon Fraser University
The human monoclonal antibody b12 neutralizes a broad range of HIV-1 primary isolates. We have identified a peptide that binds tightly and specifically to this antibody, and block its interaction with HIV-1. The structure of the b12 antibody in complex with the peptide reveals that the peptide, in part, mimics critical aspects of the b12 epitope on gp120. Immunization studies aimed at eliciting b12-like, neutralizing antibody responses with the peptide will be discussed.

4:30 Exploiting the Crystalline Surface Protein of the Bacterium Caulobacter to Display Libraries of Peptides or Genome Fragments
Dr. John Smit, Professor of Microbiology, Department of Microbiology and Immunology, University of British Columbia
Caulobacter crescentus is a harmless bacterium that produces a very useful two-dimensional crystalline assembly on its outer surface, composed of a single highly expressed protein. Because it seems to have a very flexible mechanism for exporting and assembling this protein, we have been able to present a variety of foreign peptides, ranging up to 250 amino acids in size. By inserting peptides of interest within the crystalline structure one can present about 20,000 copies/square micron (40,000 copies/cell). We have developed small, high-copy-number plasmid vectors to rapidly produce peptide or gene fragment display libraries. The high copy number and the fact that it is a bacterial display system allow ready adaptation to flow cytometry as a rapid means to detect clones of interest. Because the bacterium also spontaneously forms dense monolayer biofilms, it can be adapted to a variety of automated procedures designed to go rapidly from "hit" to sequence analysis. Following identification of interesting clones, the S-layer expression system can also serve as a peptide/protein production system by using just the S-layer secretion signal, now commercially available as PurePro™ (Invitrogen). This system also has a built-in purification mechanism. Finally, work is under way to recrystallize recombinant S-layer proteins onto inert surfaces as a first step in development of chip-based proteomic display libraries.

5:00 Use of DNA Microarrays to Deconvolute the Results of mRNA-Display Genomic Selections
Dr. Glenn F. Short III, Research Associate, HHMI, Department of Molecular Biology, Massachusetts General Hospital
Since its inception, mRNA-display has been exploited as a selection platform allowing the derivation of functional peptides and proteins from random sequence libraries. Recently, we have extended this technology to functional genomic applications by developing mRNA-display genomic libraries as tools for deciphering protein-protein interactions mediated by PDZ domains. In an effort to facilitate high-throughput proteomic screening, we have generated a 70-mer DNA microarray containing probes for all known and predicted human PDZ domains based on the SMART database (EMBL). The DNA microarray has been used successfully for the deconvolution of a model PDZ selection using the C-terminus of the NMDA receptor as bait. Instead of relying upon iterative cycles of selection/amplification, as is traditionally done in mRNA-display, we have been able to read-out the selection directly by DNA microarray analysis, thus obviating the need for DNA sequencing. These results suggest that this approach may be a viable tool for the rapid elucidation of candidate proteins from various genomic libraries and as a useful method for proteomic discovery itself.

5:30 Yeast Display Technology for the Selection of High-Affinity Human Antibodies
Dr. Michael Roguska, Abbott Bioresearch Center
Abbott Bioresearch Center (formerly BASF Pharma) and Cambridge Antibody Technology initiated a broad collaboration in 1993 under which a joint Abbott/CAT research team would use phage-display technology to discover human antibody therapeutics. The initial joint research project was directed to generation of a fully human antibody to neutralized tumor-necrosis factor (TNF). The resulting fully human antibody, D2E7 (adalimumab), which is being developed by Abbott, binds human TNF with high affinity, and potently neutralizes its biological activity in in vitro and in vivo models. Clinical trials in rheumatoid arthritis (RA) began in 1997, and Abbott plans to submit for regulatory approvals this year. Following on the success of D2E7, the first phage-derived human antibody in development, Abbott Bioresearch Center embarked on additional human antibody projects using the phage-display approach. The fully-human anti-IL12 antibody J695 is currently in Phase II clinical trials, and other discovery projects are ongoing. On some subsequent discovery projects we encountered aberrant antigen binding to phage scFv complicated affinity maturation efforts. We have utilized yeast display as an alternative technology for antibody affinity maturation. Data will be presented on the results of model selections for different antibody-antigen pairs and on the affinity maturation of an scFv using yeast display in conjunction with high-speed fluorescence-activated cell sorting (FACS) to generate high-affinity human antibodies.

6:00 Reception (sponsored by Cambridge Healthtech Institute)

7:30 Close of Day One

 

TUESDAY, APRIL 23

8:00am Poster and Exhibit Viewing and Light Continental Breakfast

 

DIRECTED PROTEIN EVOLUTION TECHNIQUES

8:30 Chairperson's Remarks
Dr. Richard Wagner, Senior Vice President, Research, Phylos, Inc.

8:35 Protein Engineering by Yeast Surface Display
Dr. K. Dane Wittrup
Yeast surface display has been used for affinity and stability maturation of antibodies and T-cell receptors with considerable success. Progress in extending this method to screening a large (~10^9) nonimmune human antibody library for novel binders will be described. Focused saturation mutagenesis strategies for affinity maturation will be compared. Application of yeast display to development of more productive protein expression systems will also be described.

9:05 Shotgun Scanning
Dr. Gregory A. Weiss, Assistant Professor of Chemistry, Department of Chemistry, University of California, Irvine
Shotgun scanning applies large libraries of phage-displayed alanine-substituted proteins for rapid mapping of protein surfaces responsible for binding. Results from shotgun scanning streptavidin will be presented, in which the contribution to binding the femtomolar ligand biotin was assessed for every streptavidin residue. In addition to shotgun scanning with alanine substitutions, other amino acid substitutions can elucidate contributions to protein functionality by specific sidechains.

9:35 Advancements in Selecting Ultrahigh-Affinity Binders Routinely Using mRNA Display Technology
Dr. Stephen P. Hale, Associate Director of Selections, Phylos Inc.
mRNA display allows for the generation of libraries of immense diversity. The potential for molecules of highly specialized function being present in such libraries is great. A thorough understanding of the parameters describing both the desired functionality and the selection system itself allows for the conditional enrichment of highly specialized molecules.

10:05 Poster and Exhibit Viewing, Refreshment Break

10:45 Construction of Combinatorial Protein Libraries by Random Multirecombinant PCR and in Vitro Screening of Novel Functional Proteins Using in Vitro Virus
Dr. Toru Tsuji, Postdoctoral Fellow, Yanagawa Unit, Mitsubishi Kagaku Institute Of Life Sciences
We have quite recently developed random multirecombinant PCR, which permits the shuffling of several DNA fragments without homologous sequences, and applied it to create two different combinatorial DNA libraries-random shuffling library and alternative splicing library. We would like to mention our recent works on the construction of combinatorial protein libraries by random multirecombinant PCR and in vitro screening of novel functional proteins using in vitro virus.

11:15 Use of T7 Phage Display to Clone RNA-Binding Proteins from cDNA Libraries
Dr. Joel Belasco, Skirball Institute of Biomolecular Medicine, New York University School of Medicine
RNA-binding proteins are central to posttranscriptional gene regulation and play an important role in a number of major human diseases. To make it easier to clone proteins that specifically bind RNA regulatory elements of interest, we have developed a rapid and broadly applicable in vitro genetic-selection method based on T7 phage display. Using defined RNAs as bait, we could selectively amplify T7 phage displaying the appropriate RNA-binding protein from a human cDNA phage library containing more than ten million independent clones. This method allows the selection even of proteins that bind their cognate RNA targets with relatively weak affinities. Of pivotal importance to the effectiveness of the strategy was the construction and use of a novel ribonuclease-deficient E. coli host strain for T7 phage growth.

11:45 Applying Phage Display to Functional Genomics
Dr. Andrew Bradbury, Biosciences Division, Los Alamos National Laboratory
Novel methods to apply phage display to the functional analysis of gene products will be presented.

12:15 Panel Discussion

12:45 Luncheon (sponsored by Cambridge Healthtech Institute)

 

GENERATION AND SELECTION OF LIGANDS AND ANTIBODIES

2:00 Chairperson's Remarks
Dr. Andrew Bradbury, Associate Professor of Medicine and Cancer Biology, University of Texas, M.D. Anderson Cancer Center

2:05 Polydactyl Zinc Finger Proteins and the Control of Endogenous Genes
Dr. Carlos F. Barbas III, The Skaggs Institute for Chemical Biology, Department of Molecular Biology, The Scripps Research Institute
In order to create a universal system for the control of gene expression, we have studied methods for the construction of novel polydactyl zinc finger proteins that recognize extended DNA sequences. Phage display and rational design were used to create a large family of zinc finger domains that may be recombined to specifically recognize most DNA sequences. Construction of polydactyl proteins containing six defined zinc finger domains and recognizing 18-bp of DNA sequence has allowed for the targeting of unique DNA addresses within the human genome. Applications of our transcription-factor approach to both disease and discovery will be presented.

2:35 From Antibodies to Peptides to Antibodies: Antagonists of IgE from Phage Display
Dr. Henry B. Lowman, Senior Scientist, Department of Protein Engineering, Genentech, Inc.
Antibodies directed against IgE, such as Xolair™, support the notion of targeting the IgE:IgE-receptor binding event as a means of treating allergic disease. Using phage display, we sifted through a panel of libraries and identified two structurally distinct peptide families, one a beta hairpin and the other a novel "zeta" fold, for binding the high-affinity receptor FceRI. Surprisingly, the two families appear to inhibit IgE activity by binding small overlapping epitopes on the receptor. These results suggest that small molecules have the potential to act as general antagonists of the allergic response. With appropriate modifications, the peptides themselves may also be therapeutically viable antagonists.

3:05 Use of Substrate Phage Display and Substrate Subtraction Phage Display to Elucidate Optimal and Selective Subsite Occupancy for Substrates of Human Fibrinolytic Serine Proteases
Dr. Ed Madison, Professor, Department of Vascular Biology, Torrey Pines Institute for Molecular Studies; and Vice President of Biological Research, Corvas International
The use of substrate phage display to elucidate optimal subsite occupancy for substrates of all three human fibrinolytic serine proteases (t-PA, u-PA, and plasmin) will be described. Modification of conventional substrate phage display to facilitate the identification of selective substrates that discriminate between intimately related enzymes that share the same primary physiological substrates and inhibitors will also be discussed.

3:35 Biosynthetic Phage Display: A Novel Protein Engineering Tool Combining Chemical and Biological Approaches
Dr. Anthony A. Kossiakoff, Professor and Chair, Department of Biochemistry and Molecular Biology, University of Chicago
Biosynthetic phage display is a method that allows selective manipulation of both genetic and chemical diversity in one protein engineering tool. It combines the ability to introduce nonnatural amino acids or altered peptide bonds into a protein using native chemical ligation with the capability for employing exhaustive targeted mutagenesis of the protein via phage display mutagenesis. This method was used to introduce a nonnatural amino acid reporter group into the interior of the protein eglin, a serine protease inhibitor, and remodel the packing and electrostatic environment around the reporter group by altering the spatially adjacent amino acids using phage display mutagenesis.

4:05 Poster and Exhibit Viewing, Refreshment Break

4:30 Profiling the Cancer Immunome Using Phage cDNA Display
Dr. Veerle Somers, Maastricht University and Dyax SA
We describe the development and application of a procedure, called "Serological Antigen Selection," for the rapid generation of a profile of tumor antigens corresponding to the humoral immune response in cancer patients. Serological Antigen Selection involves the display of cDNA expression libraries on filamentous phage and the selection with serum from cancer patients. We identified a panel of 13 different antigens and analyzed their detailed serological analysis with a panel of 150 sera from colorectal cancer patients and healthy individuals. This analysis showed that six antigens had a preferential reactivity to sera from cancer patients. Four of our antigens showed an increase in serum reactivity after vaccination with autologous tumor cells. This shows the potential of our approach to generate serological probes for monitoring of tumor-cell-based vaccination trials.

5:00 Polyclonal Antibody Libraries for Cancer and Infectious Diseases
Dr. Jackie Sharon, Professor of Pathology and Laboratory Medicine, Boston University School of Medicine
A polyclonal antibody library (PCAL) is a standardized mixture of antibodies specific for a multiantigen target, for which the genes are available and therefore the mixture can be perpetuated, amplified, and modified as desired. A PCAL contains both target-specific and cross-reactive antibodies but is designed to recognize the antigenic profile of the target over the antigenic profiles of cross-reactive multiantigens, with a high signal-to-noise ratio. PCALs are generated by positive +/- negative selection from Fab phage display libraries and mass transfer of the selected heavy- and light-chain variable region gene pairs from the phage display vector to a mammalian expression vector to produce full-length glycosylated antibodies. We have developed a system for PCAL generation and have selected Fab phage display libraries reactive with human colorectal cancer cells and with the protozoan parasite Cryptosporidium parvum. These libraries were shown to be diverse at the DNA level by fingerprint analysis and at the antigen level by immunoblot analysis and are now being transformed into full-length antibody libraries.

5:30 Antibody and Protein Arrays
Dr. Tara Heitner, Senior Scientist, Chip Technology, BioTrove Inc.
The Living Chip™ is an array of channels or throughholes (104-105) in a silicon wafer with a density comparable to standard microarray technologies but with the additional feature of isolated volumes (typically 10-100 nL in volume, 200-250 µm across, and at least 500 µm in length), each containing aqueous solutions or cells and media. At these small dimensions, fluid (containing reagents or cells) can easily be transferred into the channels and retained entirely by capillary forces due to surface functionalization. The absence of a bottom to the channels greatly simplifies reagent-loading, cherry-picking, washing steps and mixing that are currently performed in microtiter plates with complex robotics. The Living Chip™ has been applied to screening phage-display libraries in ultrahigh throughput. The advantage to performing screens in this platform are many; the most significant, however, is our ability to perform both affinity and functional screens in ultrahigh throughput and to perform several assays in parallel on the same clones. The ability to screen >106 phage clones/day in ultrahigh throughput for both affinity and functional assays will be demonstrated. This technology may be applied to all forms of display technology, many different types of assays, and combinatorial library storage.

6:00 Close of Conference


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 binder, a one-page summary must be submitted and registration must be paid in full by March 22, 2002.  Click here for poster instructions

CALL FOR SPONSORS AND EXHIBITORS
It is only through the use of phage display technology that the potential of protein engineering and proteomics can be realized. Truly, this technology can be described as a chemistry set for protein researchers in that protein properties and selectivity can be specified through the use of directed evolution. Phage display has been particularly useful in producing human antibodies. We strongly encourage any company with services or products related to phage display, antibody production, protein detection and amplification, directed evolution, proteomics, protein arrays, drug discovery, protein interaction databases, functional genomics, disease research, and ligand selection techniques to consider sponsoring or exhibiting at this event. Certainly sponsorship is the best way to prominently elevate your company's presence and influence at this conference. Although exhibit space can be purchased separately, many sponsorship packages will include a booth. The early deadline of January 18, 2002 is fast approaching-registering to exhibit before that date will save your company up to $600! For more information on sponsorship opportunities or to reserve a booth, please contact Jim MacNeil at 781-972-5441 or jmacneil@healthtech.com.

Phage Display Technologies Exhibitors:
The following companies are exhibiting as of April 20, 2002
Dyax Corporation
TSI Incorporated

Recombinant Antibodies Exhibitors:
The following companies are exhibiting as of April 20, 2002

Altus Biologics, Inc.

TSI Incorporated
Sapidyne Instruments Inc.

HOTEL INFORMATION
University Park Hotel @ MIT
20 Sidney Street
Cambridge, MA 02139
T: 617-577-0200 o 800-222-8733
F: 617-494-8366
E: reservations@hotelatmit.com

Room Rates: $195/S o $205/D
Cut-off-Date: April 1, 2002

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.

TRAVEL INFORMATION
Special Airline Discounts Available
Special zone and discount fares have been established on United Airlines for this conference. Please call United Airlines Meeting Reservations Center directly at 800-521-4041. You must reference ID #579YS.

 

 

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