Cytogen Corporation

Other

Cytogen Corporaton

Thomas J McKearn

John D Rodwell

Vernon L Alvarez

Chyi Lee

John W Goers

Daniel J Coughlin

Jean P Ripoll

Hurley D King

Gerard A Quash

Richard C Siegel

Robert D Radcliffe

Cynthia G Long

A system or method for identifying and/or designing novel peptides and polypeptides comprising an amino acid sequence which mimics the molecular recognition site of either (a) a macromolecule such as an immunoglobulin, an enzyme, a receptor protein, a lectin or other binding protein or (b) a small molecule or a small region of a large molecule which functions as a ligand and is recognized and binds specifically to a macromolecule is disclosed. Novel peptides and polypeptides as well as conjugates of the peptides and polypeptides are also disclosed. Applications for use of the peptides, polypeptides and conjugates in a wide range of fields such as biomedicine; biological control and pest regulation; agriculture; cosmetics; environmental control and waste management; chemistry; catalysis; nutrition and food industries; military uses; climate control, etc. are disclosed.

Molecular recognition units

The invention relates to amine-containing porphyrin derivatives. Theporphyrins can be used as photosensitizers which are useful as therapeutic agents. Also described are methods for preparing conjugates in which a porphyrin derivative is covalently attached to an antibody or antibody fragment. In vivo therapeutic methods utilizing the conjugates are also desired.

Amine-containing porphyrin derivatives

Novel and improved antibody compositions comprising an antibody or antibody fragment having an increased number of sites on a carbohydrate side chain available for the site specific attachment of a compound to a region of the antibody or antibody fragment which is not part of nor directly involved with the antigen binding site are disclosed. Conjugates, prepared using the high-mannose-containing antibodies, which are characterized by substantially the same immunospecificity as the unmodified unconjugated antibody molecule, are also disclosed. The antibody compositions are advantageously used for a wide variety of therapeutic and diagnostic applications in both in vivo and in vitro targeted delivery systems and assays. Methods for preparing the antibody compositions, as well as antibody conjugate intermediates, and methods for using the antibody compositions are also described.

Novel and improved antibodies for site specific attachment of compounds

Novel and improved methods for diagnosis, prognosis, prophylaxis and therapy of viral infections are described. The novel methods employ a virus, viral antigen or fragment thereof in which 'perturbation' of an oligosaccharide moiety renders the virus, viral antigen or fragment thereof more specifically recognizable or reactive with neutralizing antibody. As described, 'perturbation' of an oligosaccharide moiety encompasses a variety of modifications such has one that (1) alters the chemical or physical structure of a carbohydrate residue that is naturally present; (2) that removes, wholly or in part, a carbohydrate residue; and/or (3) that prevents or alters addition of a carbohydrate residue. A variety of different methods for oligosaccharide 'perturbation' are also described. In particular, the carbohydrate residue is altered by an oxidizing agent.

Oxidized viruses or viral antigens and utilization for diagnostic

This invention relates to antibody-therapeutic agent conjugates having a therapeutic agent covalently attached to an antibody or antibody fragment. Also described are methods for intermediates in the preparation of antibody conjugates. Therapeutic in vivo methods utilizing such antibody-therapeutic agent conjugates are described.

Antibody-therapeutic agent conjugates

Novel and improved methods for diagnosis, prognosis, prophylaxis and therapy of viral infections are described. The novel methods employ a virus, viral antigen or fragment thereof in which 'perturbation' of an oligosaccharide moiety renders the virus, viral antigen or fragment thereof more specifically recognizable or reactive with neutralizing antibody. As described, 'perturbation' of an oligosaccharide moiety encompasses any modification that (1) alters the chemical or physical structure of a carbohydrate residue that is naturally present; (2) that removes, wholly or in part, a carbohydrate residue; and/or (3) that prevents or alters addition of a carbohydrate residue. A variety of methods for oligosaccharide 'perpetuation' are also described.

Carbohydrate perturbations of viruses or viral antigens and utilization

This invention relates to antibody-metal ion complexes having a metal ion coordinately bound to a compatible chelator covalently bound to an antibody or antibody fragment. Also described are methods for intermediates in the preparation of antibody-metal ion complexes. Therapeutic and in vitro and in vivo diagnostic methods utilizing such antibody-metal ion complexes are described.

Antibody-metal ion complexes

A method is described for the covalent attachment of linker groups to specific sites on antibody molecules directed against any desired target antigen (tumor, bacterial, fungal, viral, parasitic etc.). These linkers can be attached via amide or ester bonds to compounds for delivery which contain available amino or hydroxy groups (e.g., bioactive agents, cytotoxic agents, dyes, fluors, radioactive compounds, etc.). In addition the linkers can be incorporated into insoluble matrices for use in separation schemes which are based upon antibody-antigen interactions. The linkers may be designed so that they are susceptible to cleavage by any one of the serum complement enzymes. When prepared according to the methods described herein, the resulting modified antibody molecule retains the ability to bind antigen and to fix serum complement. Thus, when administered to a patient the antibody conjugate binds to its target in vivo. As a result of the subsequent activation of the patient's serum complement, the covalently attached compound will be specifically cleaved at the target site by the proteolytic enzymes of the complement system.

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New Hope, PA, United States of America

Thomas J McKearn