The present application generally relates to multi-specific molecules that bind to multiple bacterial virulence factors, methods for producing these binding molecules, and the use of these binding molecules to treat bacterial infections. In particular, the binding molecules comprise at least two binding domains, preferably an antibody or antibody fragment and an alternative scaffold. The first binding domain is capable of binding to a glycosylated staphylococcal surface protein, preferably an SDR-containing protein. The second binding domain is capable of binding to a staphylococcal leukotoxin, preferably LukAB, LukD or LukE. These multi-specific binding compounds have killing activity against staphylococci and, thus, can be used in the treatment and/or amelioration of a Staphylococcus infection, including methicillin-resistant Staphylococcus aureus.

We described a novel system of targeted cell therapy with a protein toxin, such as anthrax toxin, that has been modified to re-direct it to a desired cell target instead of its natural cell target. The system can be used for, e.g., targeted killing of undesired cells in a population of cells, such as cancer or overly active immune system cells.

Provided herein are compounds and compositions having antibiotic activity against methicillin resistant Staphylococcus aureus (MRSA). In particular, provided herein is a synbody that bactericidal against multiple strains of MRSA and that can be used in conjugation with currently approved -lactam antibiotics to treat MRSA strains having resistance to -lactam treatment. Also provided are methods of using the compounds and compositions for treating, preventing or reducing MRSA infections.

The present application generally relates to multi-specific molecules that bind to multiple bacterial virulence factors, methods for producing these binding molecules, and the use of these binding molecules to treat bacterial infections. In particular, the binding molecules comprise at least two binding domains, preferably an antibody or antibody fragment and an alternative scaffold. The first binding domain is capable of binding to a glycosylated staphylococcal surface protein, preferably an SDR-containing protein. The second binding domain is capable of binding to a staphylococcal leukotoxin, preferably LukAB, LukD or LukE. These multi-specific binding compounds have killing activity against staphylococci and, thus, can be used in the treatment and/or amelioration of a Staphylococcus infection, including methicillin-resistant Staphylococcus aureus.

The present disclosure relates to compositions and methods comprising peptide molecules that mimic the binding and functional properties of native antibodies relative to their respective targets. Some embodiments comprise peptide-drug conjugates (PDCs) comprising the mimic peptides disclosed herein. The targets of these mimic peptides include epidermal growth factor receptor (EGFR), and human epidermal growth factor receptor 2 (HER2), vascular endothelial growth factor (VEGF), programmed cell death protein 1 (PD-1), and programmed death-ligand 1 (PD-L1). The present disclosure comprises application of the knob-socket computational model to design antibody mimics for proteins.

A substrate may be disposed on a substrate support in a flood exposure treatment system. A flood exposure dose profile may be selected. The substrate may be exposed to flood irradiation from a source, and the flood irradiation may be terminated when the selected flood exposure dose profile is achieved. Exposing the substrate to flood irradiation may comprise controlling at least one of a substrate rotation rate, a source scanning rate, a substrate scanning rate, a source power setting, a distance from the source to the substrate, a source aperture setting, an angle of incidence of flood irradiation on the substrate, and a source focus position to achieve the selected flood exposure dose profile.

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).

This invention concerns anti-inflammatory agents, compositions, and methods for treating inflammatory disorders.

The application relates to a dual cytokine fusion protein composition, pharmaceutical composition, and/or formulation thereof comprising IL-10 or IL-10 variant molecules fused to a single chain variable fragment scaffolding system and a second cytokine, where the second cytokine is linked in the hinge region of the scFv. The application also relates to methods of using the dual cytokine fusion protein composition for treating cancer, inflammatory diseases or disorders, and immune and immune mediated diseases or disorders.

The present invention provides new anti-SIRPa antibodies able to specifically antagonize the interaction between SIRPa and CD47, without affecting the interaction between SIRPg and CD47, and their uses.