44 results about "IgG binding" patented technology

Antibodies to heavy chain of human FcRn are provided which function as non-competitive inhibitors of IgG binding to FcRn. The antibodies may be polyclonal, monoclonal, chimeric or humanized, or antigen binding fragments thereof. These antibodies are useful for reducing the concentration of pathogenic IgGs in individuals and therefore used as a therapeutic tool in autoimmune and alloimmune conditions.

The invention involves viral vectors that can be used to tranduce a target cell, i.e. to introduce genetic material into the cell. The targets of interest are eukaryotic cells and particularly human cells. The transduction can be done in vivo or in vitro. More particularly the invention concerns viral vectors that have chimeric envelope proteins and contain the IgG-binding domain of protein A. These vectors when used in conjunction with antibodies targeting a particular cell are particularly useful for gene therapy.

It has been determined that allergens, which are characterized by both humoral (IgE) and cellular (T cell) binding sites, can be modified to be less allergenic by modifying the IgE binding sites. The IgE binding sites can be converted to non-IgE binding sites by masking the site with a compound that prevents IgE binding or by altering as little as a single amino acid within the protein, most typically a hydrophobic residue towards the center of the IgE-binding epitope, to eliminate IgE binding. The method allows the protein to be altered as minimally as possible, other than-within the IgE-binding sites, while retaining the ability of the protein to activate T cells, and, in some embodiments by not significantly altering or decreasing IgG binding capacity The examples use peanut allergens to demonstrate alteration of IgE binding sites. The critical amino acids within each of the IgE binding epitopes of the peanut protein that are important to immunoglobulin binding have been determined. Substitution of even a single amino acid within each of the epitopes led to loss of IgE binding. Although the epitopes shared no common amino acid sequence motif, the hydrophobic residues located in the center of the epitope appeared to be most critical to IgE binding.

In certain embodiments, the present invention provides novel antibody purification methods and systems using a potentially simple and cost-efficient means. In some embodiments, customized Z-33 derived from Staphylococcus aureus Protein A is used to construct immuno-amphiphile molecules which can assemble into immunofibers in aqueous solution with bioactive epitopes on the surface and have IgG binding ability.

The invention discloses a class of small proteins and applications thereof. The backbone protein of the small protein is a mutant of the IgG-binding domain of Streptococcal protein G, and the small protein includes an alpha-helix and four beta-sheets, the alpha-helix running through a region surrounded by four beta-sheets , and at the same time, key amino acid sites capable of binding to PD-1 protein are also distributed on the β-sheet surface formed by the four β-sheets. The small protein of the present invention has a high structural similarity with PD‑L1 protein, can inhibit PD‑1 / PD‑L1 binding, and is a potential PD‑1 / PD‑L1 inhibitor, which has weak IgG binding ability and can be used in vivo The circulation residence time is long, and has high structural stability, can be used to inhibit the interaction between PD‑1 / PD‑L1, is simple to prepare, can be used for large-scale production and application, and facilitates the immunotherapy of cancer.