Medical Research Council

Cambridge Antibody Technology Limited

Other

Domantis Limited

Medimmune Limited

The Scripps Research Institute

Btg International Limited

Stratagene

Philogen S.p.a.

Glaxo Group Limited

British Technology Group Limited

Cancer Research Technology Limited

Celltech Limited

Biacore Ab

Bicyclerd Limited

Gregory Paul Winter

Andrew David Griffiths

James David Marks

Kevin Stuart Johnson

John Gerald McCafferty

Lutz Riechmann

Anthony Richard Pope

Ronald Henry Jackson

Kaspar Philipp Holliger

Timothy Peter Bonnert

David John Chiswell

Timothy Piers Clackson

Richard A Lerner

Joseph A Sorge

Dario Neri

Christian Heinis

Geoffrey Walter Grigg

Hendricus Renerus Jacobus Mattheus Hoogenboom

Henricus Renerus Jacobus Mattheus Hoogenboom

David Loakes

Elise Bernard

Andrew John Smith

William D Huse

Peter Michael Waterhouse

Magnus Malmqvist

Rudolf M T De Wildt

Marina Vaysburd

Daniel Paul Teufel

Steve Holmes

Brian Timothy McGuinness

Ian M Tomlinson

Armin Sepp

Luciano Zardi

Benjamin P Woolven

Barbara Carnemolla

Mary Frances Fitzgerald

Justian Craig Fox

Elizabeth Sally Ward

Robert E Hawkins

Hendricus Renerus Hoogenboom

Ahuva Nissim

Peter Kristensen

Jean-Luc Jestin

Jennifer A Lee

Andrew John Hammond Smith

Terence Derek Prospero

Jennifer Luckett

Herman Waldmann

Laurent Stephane Jespers

Michael Ronald Clark

Dan S Tawfik

John Tite

Stephen J Russell

Francesca Viti

Samuel Cameron Williams

Adrian Huber

Salvatore Demartis

Detlef G&uuml;ssow

Hendricus Renerus Jacobus Matheus Hoogenboom

Kaspar-Philipp Holliger

Dennis Raymond Burton

Alexander Robert Duncan

Stephen James Russell

Tristan J Vaughan

Alison Jane Wilton

Philip Ronald Tempest

Philip Jones

Mark William Bodmer

Oliver Schon

Raymond John Owens

Geoffrey Thomas Yarranton

Michael Baier

Andrew James Williams

Freda Stevenson

Julia Elizabeth Thompson

Claudia De Lalla

Thomas Martin Simon

Igor Fisch

Peter T Jones

Guy Gorochov

Louise Bacon

Henricus Renerus Hoogenboom

Michael J Embleton

Kaspar-Philip Holliger

Delin Zhu

Detlef Güssow

Steven Paul Ruddock

Raymond Paul Field

Jonathan Alexander Green

Hendricus Reneus Jacobus Mattheus Hoogenboom

Kasper Philipp Holliger

Leo C James

Lutz Reichmann

John Paul Tite

Hendricus Renerus Jacobus M Hoogenboom

The invention relates to a complex comprising a phage particle, said phage particle comprising

Methods and compositions

The invention relates to a method for providing a multispecific peptide ligand comprising a polypeptide covalently linked to a molecular scaffold at three or more amino acid residues and capable of binding to two or more separate targets, comprising the steps of: (a) providing a first repertoire of polypeptides, each polypeptide comprising two or more reactive groups capable of covalent linkage to a molecular scaffold, and at least one loop which comprises a sequence of two or more amino acids subtended between two of said reactive groups; (b) providing a second repertoire of polypeptides as described in (a); (c) joining at least one loop of one or more members of the first repertoire to at least one loop of one or more members of the second repertoire to form at least one polypeptide comprising two loops, and (d) conjugating the composite polypeptide(s) to a molecular scaffold at at least three amino acid positions.

Multispecific peptides

Connector compound peptide phage display

The invention relates to a method for modifying one or more peptide ligands, comprising polypeptides covalently linked to a molecular scaffold at two or more amino acid residues, comprising the steps of providing one or more peptide ligands, wherein the polypeptide comprises two or more reactive groups which form a covalent linkage to the molecular scaffold, and at least one loop which comprises a sequence of two or more amino acids subtended between two of said reactive groups; exposing the peptide ligands to one or more proteases; and sorting the ligands according to the extent of proteolytic cleavage.

Structured peptide processing

Disclosed is the use of an agent (e.g., antibody fragment, antagonist, ligand, dAb monomer) that binds a target in pulmonary tissue for the manufacture of a long action or long therapeutic window formulation for local delivery to pulmonary tissue, and methods for administering an agent that binds a target in pulmonary tissue to a subject to produce a long therapeutic window in pulmonary tissue. The formulation is for, and the method comprises, administering locally to pulmonary tissue. Also disclosed is the use of antagonists of TNFR1 for the manufacture of a formulation or medicament for treating, preventing or suppressing lung inflammation or a respiratory disease, and methods of treating such diseases. Also disclosed are the use of agents a for the manufacture of a delivery device (e.g., inhaler, intranasal delivery device) for the treatment or prevention of lung inflammation or a respiratory disease, and a delivery device for the treatment or prevention of lung inflammation or a respiratory disease that contains an agent as described herein.

Methods for targeting pulmonary diseases with agents that bind a target in pulmonary tissue

The invention relates to a method for altering the conformational diversity of a first repertoire of polypeptide ligands, comprising a plurality of polypeptides comprising at least two reactive groups separated by a loop sequence covalently linked to a molecular scaffold which forms covalent bonds with said reactive groups, to produce a second repertoire of polypeptide ligands, comprising assembling said second repertoire from the polypeptides and structural scaffold of said first repertoire, incorporating one of the following alterations: (a) altering at least one reactive group; or (b) altering the nature of the molecular scaffold; or (c) altering the bond between at least one reactive group and the molecular scaffold; or (d) any combination of (a), (b) or (c).

Peptide libraries

According to the present invention there is provided a specific binding member which is specific for and binds directly to the ED-B oncofoetal domain of fibronectin (FN). The invention also provides materials and methods for the production of such binding members.

Antibodies of the ED-B domain of fibronectin, their construction and uses

The present invention concerns a method for the selection of a virus comprising the steps of: (a) providing a virus encoding and displaying a fusion polypeptide, said fusion polypeptide comprising a heterologous polypeptide inserted into the sequence of a viral coat protein polypeptide, wherein said virus comprises a cleavable site located within a displayed polypeptide; (b) exposing the virus to a cleaving agent; (c) propagating the virus comprising intact fusion protein.

Selection system

The present invention relates to a method for isolating from the immunological gene repertoire a gene coding for a receptor having the ability to bind a preselected ligand. Receptors produced by the gene isolated by the method, particularly catalytic receptors, are also contemplated.

Method for producing polymers having a preselected activity

An inhibitor of the aggregation of immunoglobulin chains is provided. The inhibitor may comprise or consist of a polypeptide which comprises or consists of (a) an amino acid sequence corresponding to the amino acid sequence of the FR1 region of an immunoglobulin light chain variable domain, or part thereof which includes amino acid residue 12, (b) an amino acid sequence corresponding to the amino acid sequence of the immunoglobulin-binding domain of bacterial superantigen Protein L, or part thereof, and/or (c) an amino acid sequence corresponding to the amino acid sequence of the immunoglobulin-binding domain of streptococcal protein G, or part thereof, or a variant, fusion or derivative thereof, or a fusion of a variant or derivative thereof which retains the ability of the parent polypeptide to inhibit aggregation of immunoglobulin chains, or domains thereof. Other versions of the inhibitor are also provided.

Prevention of aggregation of immunoglobulin light or heavy chains

Agents that bind a target in pulmonary tissue for targeting respiratory diseases

Growing community of inventors

Cambridge, United Kingdom

Gregory Paul Winter