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Biotech / Medical : Cambridge Antibody Technology Group -- Ignore unavailable to you. Want to Upgrade?

To: michael_f_murphy who wrote (7)	1/6/2000 7:59:00 PM
From: michael_f_murphy	Respond to of 625

US 5,885,793 "Production of Anti-Self Antibodies from Antibody Segment Repertoires and Displayed on Phage" 24 March 1999 Melbourn, UK... Cambridge Antibody Technology ("CAT") has been granted a US patent with broad claims covering human antibodies to human proteins isolated by phage display. The key significance of the patent is that it covers the isolation of human antibodies against all human proteins, except for those that generate natural antibodies in humans. Targets for drugs designed to treat many human diseases will often be such human proteins, particularly as future drug targets emerge from human genome initiatives. Dr David Chiswell, Chief Executive Officer of CAT, commenting on today's announcement, said: "This provides CAT with a fundamental US patent which significantly strengthens our intellectual property position in the US and adds to our patent portfolio in both the US and Europe covering the isolation of monoclonal antibodies by phage display. In particular, the patent's broad coverage, of human antibodies that bind human proteins, underpins our business strategy of developing a broad pipeline of human antibody based therapeutic products." This patent, No. US 5,885,793, entitled "Production of Anti-Self Antibodies from Antibody Segment Repertoires and Displayed on Phage" arises from work carried out by the Medical Research Council ('MRC') and CAT. This work demonstrated that human antibody fragments directed against human proteins could be isolated from human antibody phage display libraries constructed from non-immunised humans. An equivalent Australian patent has already been granted, with European and Japanese filings currently under examination.

To: michael_f_murphy who wrote (7)	1/6/2000 10:25:00 PM
From: michael_f_murphy	Read Replies (1) \| Respond to of 625

Re: Aptein & polysome display (patents & technology) Press release regarding Aptein patents Aptein Inc., has been issued two United States patents, entitled "Cell-Free Synthesis" and "Isolation of Novel Genes and Polypeptides," that broadly cover methods to screen over 10^12 random polypeptides in small volumes. These patents describe a technology that utilizes in vitro translation to produce large libraries of "polysomes" that allow for the recovery of high-affinity binders against receptors and other targets. This cell-free process involves polysome particles that contain a randomly generated polypeptide plus the genetic material coding for the peptide (mRNA), and one or more ribosomes engaged in protein synthesis. The polysomes bind via the peptides or proteins to targets of pharmaceutical interest and the associated genes can be rescued by gene amplification. A single polypeptide binding event may be detected and the sequence may be recovered with this invention. Typically, three or four rounds of polysome selection are serially performed to enrich for the highest affinity molecules, which are identified by DNA sequencing and binding assays. The terms, "polysome display" and "ribosome display," have been used to describe the same process. Some info for self education fom Medline: 1 NLM CIT. ID: 94377484 TITLE: An in vitro polysome display system for identifying ligands from very large peptide libraries. AUTHORS: Mattheakis LC; Bhatt RR; Dower WJ AUTHOR AFFILIATION: Affymax Research Institute, Palo Alto, CA 94304. PUBLICATION TYPES: JOURNAL ARTICLE LANGUAGES: Eng REGISTRY NUMBERS: 0 (Antibodies, Monoclonal) 0 (DNA Primers) 0 (Endorphins) 0 (Epitopes) 0 (Ligands) 0 (Peptides) 0 (Recombinant Fusion Proteins) 74913-18-1 (Dynorphins) 83335-41-5 (rimorphin) ABSTRACT: We have used an in vitro protein synthesis system to construct a very large library of peptides displayed on polysomes. A pool of DNA sequences encoding 10(12) random decapeptides was incubated in an Escherichia coli S30 coupled transcription/translation system. Polysomes were isolated and screened by affinity selection of the nascent peptides on an immobilized monoclonal antibody specific for the peptide dynorphin B. The mRNA from the enriched pool of polysomes was recovered, copied into cDNA, and amplified by the polymerase chain reaction (PCR) to produce template for the next round of in vitro synthesis and selection. A portion of the amplified template from each round was cloned into a filamentous phagemid vector to determine the specificity of peptide binding by phage ELISA and to sequence the DNA. After four rounds of affinity selection, the majority of clones encoded peptides that bound specifically to the antibody and contained a consensus sequence that is similar to the known epitope for the antibody. Synthetic peptides corresponding to several of these sequences have binding affinities ranging from 7 to 140 nM. The in vitro system described here has the potential to screen peptide libraries that are three to six orders of magnitude larger than current biological peptide display systems. NLM PUBMED CIT. ID: 7522328 SOURCE: Proc Natl Acad Sci U S A 1994 Sep 13;91(19):9022-6

To: michael_f_murphy who wrote (7)	5/30/2000 7:35:00 AM
From: nigel bates	Read Replies (1) \| Respond to of 625

From healthtech.com (thanks Jongmans) " ... Protein Chips and Phage Display Dr. Scott Chappel, Senior Vice President of Research, Dyax Corporation Gene chip technology has allowed scientists to measure rates of the transcription of a collection of a large number of genes at once after a specific stimulus. While valuable, the accumulation of this information does not provide a complete picture of cellular responses to stimuli. This is due to the fact that the measurement of rates of gene transcription, may not always reflect the cell's response to a perturbation. Many stimuli are known to activate or deactivate existing proteins (for instance by phosphorylation or dephosphorylation) with no measurable change in expression rate of these proteins. An ideal method to study the responses of a cell to a stimulus would provide the ability to identify changes in the absolute amounts of specific proteins, as well as detect changes in the co- and post-translational modifications of those proteins. This can be accomplished by the identification of binding proteins to all intracellular proteins, and attaching them in a microarray format in a fashion analogous to gene chips. Such binding proteins with a high degree of specificity can be obtained through the use of phage display technology. Using this technology, antibodies can be made (completely in vitro) to any target. Moreover, selection methods allow for the identification of phage antibodies that recognize specific co- and/or post-translational modifications of the same protein. There are obvious synergies between the use of microarray chip technology and phage display isolation of specific binders to specific proteins. These technologies can be exploited to build protein chips that can quantitate changes in hundreds of proteins at once following any perturbation. Our efforts in this area will be discussed."