The disclosure relates to Angiopoietin-1 mimetics for treating vascular diseases via agonistic activation of Tie2/TEK receptor.

Methods of making engineered protein-based materials, nanofibers, and biofilms from bacterial amyloid-based structures that are capable of mediating long-range electron transport are provided.

The invention relates to truncated growth factors and variants thereof. The invention also relates to methods of making and using the truncated growth factors. The invention further relates to compositions including a protease and a growth factor comprising a bone morphogenic protein (BMP) or a variant thereof. The invention also relates to methods of using the composition.

Peptides that specifically bind erythrocytes are described. These are provided as peptidic ligands having sequences that specifically bind, or as antibodies or fragments thereof that provide specific binding, to erythrocytes. The peptides may be prepared as molecular fusions with therapeutic agents, tolerizing antigens, or targeting peptides. Immunotolerance may be created by use of the fusions and choice of an antigen on a substance for which tolerance is desired.

A first Fab region-binding peptide includes an amino acid sequence selected from the group consisting of SEQ ID NOs: 1 to 5 with substitution of one or more amino acid residues at the 17.sup.th position and the 36.sup.th position, wherein an acid dissociation pH thereof is shifted to a neutral side. A second Fab region-binding peptide further includes deletion, substitution and/or addition of one or more amino acid residues at positions other than the 17.sup.th position and the 36.sup.th position. A third Fab region-binding peptide includes an amino acid sequence with a sequence identity of 80% or more to the amino acid sequence of the first Fab region-binding peptide.

Methods for the rapid elimination of carbon monoxide (CO) from CO-bound hemoglobin, myoglobin and cytochrome c oxidase in subjects with CO poisoning are described. The disclosed therapy involves the use of rationally designed, modified, regulator of CO metabolism (RcoM) proteins and pharmaceutical compositions thereof, which scavenge carbon monoxide from poisoned tissue. The recombinant RcoM compositions are infused into blood, where they rapidly sequester carbon monoxide and limit the toxic effects of carbon monoxide on cellular respiration, oxygen transport and oxygen utilization.

Provided herein are mammalian cells comprising a first exogenous nucleic acid encoding a DNAse protein and a second exogenous nucleic acid encoding another DNAse protein, such as DNASE1 protein and DNASE1L3 protein, that have improved properties, including the ability to degrades extracellular chromatin and remove Neutrophil Extracellular Traps (NETs). Use of these cells, including the use in the treatment of a subject in need thereof, is also contemplated.

An scFv-Fc dimer binds and neutralizes TGFβ1 selectively and with high affinity and avidity. The scFv region may comprise the same VH and VL domains or CDR regions as metelimumab. The unique combination of their smaller size, high selectivity, potency against TGFβ1, and long in vivo half-life makes the scFv-Fc dimers ideal candidates for therapeutic applications.

An object of the present invention is to provide a cell penetrating peptide having a penetrating ability into cells. The present inventors provided a cell penetrating peptide consisting of the amino acid sequence of SEQ ID NO: 1, a cell penetrating peptide consisting of the amino acid sequence of SEQ ID NO: 2 and a cell penetrating peptide consisting of the amino acid sequence of SEQ ID NO: 3; and a complex comprising any one of the cell penetrating peptide and a functional molecule.

Provided are a TEV protease variant, a fusion protein thereof, a preparation method therefor and the use thereof. Provided are a TEV protease variant with unique properties obtained by screening and a fusion protein thereof. The TEV protease variant has a low enzyme cleavage activity during expression in hosts, and preferably has a lower enzyme cleavage activity compared to an S219V variant having an amino acid sequence as shown in SEQ ID NO: 10. The enzyme cleavage site of the TEV protease variant is selected from EXXYXQG/S/H, wherein X is any amino acid residue, and the enzyme cleavage site is preferably selected from SEQ ID NO: 7 and 8. Fusion expression using the TEV protease variant of the present invention and a polypeptide can be used for preparing a polypeptide quickly and efficiently, thereby solving the problems currently present in the process of the recombinant production of a polypeptide.