The present invention provides soluble RAGE-Fc fusion proteins with increased stability and extended half-life capable of binding endogenous RAGE ligands with high apparent affinity. The present invention also provides methods of making and using stable, soluble RAGE-Fc fusion proteins. These soluble RAGE-Fc fusion proteins are useful as therapeutics based on their ability to bind endogenous RAGE ligands.

The invention relates to the field of immunology and immuno-oncology. More specifically, the invention relates to multi-specific and bi-specific cytokine and antibody derivatives capable of cell and/or tissue targeting to locally enhance the immune response and to reduce systemic toxicity.

The present disclosure provides a method of treating cardiometabolic syndrome (CMS) with a GDF15 molecule. Also provided herein is a method of treating a cardiac or heart condition. In some embodiments, the GDF15 molecule is a GDF15-Fc fusion, in which a GDF15 region is fused to an Fc region, optionally via a linker.

The present invention is concerned with a protein oligomer comprising (i) at least two NC-monomers of collagen 18 or (ii) at least two endostatin domains of collagen 18 or (iii) at least two N-terminal peptides of the collagen 18 endostatin domain, for use in treating, ameliorating or preventing fibrosis or a fibrosis-associated disease, a vascular endothelial growth factor (VEGF)-related disease or a matrix metalloproteinase (MMP)-related disease. The invention further relates to the mentioned protein oligomer for use for detecting and/or diagnosing fibrosis or a fibrosis-associated disease, a vascular endothelial growth factor (VEGF)-related disease or a matrix metalloproteinase (MMP)-related disease.

The present disclosure provides polypeptides derived from SARS-CoV-2 which have therapeutic use. One such polypeptide is a polypeptide, referred to as “Npep2,” is derived from the SARS-CoV-2 protein N and has at least 50 consecutive amino acids of the amino acid sequence having at least 90% identity with the amino acid sequence that ranges from the residue at position 276 to the residue at position 411 of SEQ ID NO:2. Further described are conjugates wherein a heterologous polypeptide is conjugated or fused to Npep2. The present disclosure further provides vaccines employing the polypeptides, polynucleotides encoding the polypeptides, and methods of vaccinating subjects against SARS-CoV-2 by administering a therapeutically effective amount of one or more of the polypeptides.

Provided is a method of purifying a mixture of Fc-containing bioactive peptides by using an affinity column including an affinity matrix containing a protein A ligand, wherein the mixture of Fc-containing bioactive peptides includes a first Fc-containing bioactive peptide and a second Fc-containing bioactive peptide, and the second Fc-containing bioactive peptide includes at least one more human VH3 domain, compared to the first Fc-containing bioactive peptide. According to the purification method, bioactive peptides having the same or similar structures can be precisely separated to the high level of purity while simplification of the process is achieved.

Provided is a pharmaceutical formulation comprising a modified IL-7 protein. More particularly, it comprises (a) a modified IL-7 fusion protein; (b) a basal buffer with a concentration of 10 to 50 mM; (c) a sugar with a concentration of 2.5 to 5 w/v %; and (d) a surfactant with a concentration of 0.05 to 6 w/v %. Such pharmaceutical formulation of a modified IL-7 fusion protein does not show aggregates formation, but shows protective effects on proteins under stress conditions such as oxidation or agitation, and thus can effectively be used for the treatment of a patient.

Disclosed herein are compositions and methods for increasing the stability of recombinant nanobodies. Also disclosed herein are recombinant nanobodies comprising an IL-2 polypeptide that bind serum albumin and uses thereof for treating cancers.

The disclosure relates to compositions and methods of generating synthetic antigen receptors or SAR (e.g., SIR, zSIR, cTCR, ab-TCRs, AABD-TCRs, TFP, TACs etc.) and antibodies (e.g., bispecific antibodies, DARTs etc.) comprising one or more novel antigen binding domains. SARs as described comprise single chain immune receptors (e.g., 1.sup.st, 2.sup.nd and 3.sup.rd generation chimeric antigen receptors, TFPs. Tri-TAC and the like) and multiple chain immune receptors (e.g., SIR, zSIR, cTCR. ab-TCR. AABD-TCR. αβTFP, ydTFP, recombinant TCRs etc.). SARs are able to redirect immune cell specificity and reactivity toward one or more selected targets exploiting the antigen-binding domain properties.

The present invention relates to methods of overcoming the resistance to an EGFR (Epidermal Growth Factor Receptor)-targeting antibody through a peptide that binds specifically to neuropilin-1 (NRP1). Moreover, the present invention relates to a fusion antibody in which a peptide that binds specifically to NRP1 is fused to an EGFR-targeting antibody, and to a composition of overcoming the resistance to an EGFR-targeting antibody alone by co-administration of the EGFR-targeting antibody and an NRP1-binding peptide-fused Fc. In addition, the fusion antibody according to the present invention, in which the NRP1-specific binding peptide is fused to an EGFR-targeting antibody, overcomes the resistance to the EGFR-targeting antibody alone in pancreatic cancer. Furthermore, the fusion antibody, in which the NRP1-specific binding peptide is fused to the EGFR-targeting antibody, also overcomes resistance to the EGFR-targeting antibody alone even in lung cancer. Thus, the NRP1-specific binding-fused EGFR-targeting antibody according to the present invention may be highly effective in the treatment of various tumors resistant to EGFR-targeting antibody alone.