Circular handed alpha-helical repeat proteins are described. The repeat proteins have a number of uses as scaffolds for geometrically precise, arrayed presentation of cell-signaling or immune-related protein and peptide epitopes, as well as numerous other therapeutic, diagnostic, and nanotechnological uses.

Compositions and methods are provided for metabolically degrading ADMA. In one embodiment a device is provided for reducing a patients ADMA levels in their blood wherein the device comprises a biologically active dimethylarginine dimethylaminohydrolase (DDAH) polypeptide covalently linked to a solid support. In one embodiment a method for reducing ADMA levels in a patients blood comprises the step of contacting the patients blood or a blood fraction with an immobilized biologically active DDAH polypeptide, wherein contact of the patients blood with said DDAH polypeptide results in degradation of ADMA present in the patients blood.

The present disclosure relates generally to compositions and methods useful for the production of engineered antibodies having (i) multiple antigen-binding specificities and (ii) Fc regions that have been modified to promote heterodimer formation between heavy chains from antibodies with different specificities. Also provided are recombinant cells, recombinant nucleic acids encoding such engineered antibodies, as well as pharmaceutical compositions containing same.

Provided herein are fusion proteins, isolated nucleic acids encoding a fusion protein, and gene delivery vectors comprising the same, wherein the isolated nucleic acids comprise: (i) a first sequence encoding a RNA-binding zinc finger domain; and (ii) a second sequence encoding a fusion partner; and methods of using the same.

The present invention addresses the problem of providing: a fusion protein or conjugated protein having excellent cell membrane permeability, containing a partial peptide derived from human, and suitable for intracellular delivery; an intracellular delivery carrier comprising such a fusion protein or conjugated protein; a partial peptide; a cell membrane permeation enhancer comprising the partial peptide; DNA; and a vector. The fusion protein or conjugated protein has a partial peptide comprising at least seven consecutive amino acid residues of an amino acid sequence encoded by a predetermined DNA, and a ligand directly or indirectly bound to the partial peptide and having the capability of binding to cell surfaces. The ligand is preferably an antibody. The intracellular delivery carrier comprises the fusion protein or conjugated protein. The cell membrane permeation enhancer comprises the partial peptide.

The present invention relates to esterases, more particularly to esterase variants having improved activity and/or improved themostability compared to the esterase of SEQ ID NO:1 and the uses thereof for degrading polyester containing material, such as plastic products. The esterases of the invention are particularly suited to degrade polyethylene terephthalate, and material containing polyethylene terephthalate.

A polypeptide mimicking epitope of glycoprotein gp120 of HIV-1 virus that is recognized by a paratope of broadly neutralizing antibody VRC01 and has the length up to 100 amino acid residues and contains an amino acid sequence:

TABLE-US-00001 (SEQ ID NO. 1): X.sup.1YKNX.sup.2INX.sup.3AX.sup.4X.sup.5VX.sup.6X.sup.7VKRX.sup.8IDX.sup.9ILAX.sup.10LP X.sup.1 is selected from amino acids A, N, R; X.sup.2 is selected from amino acids A, R, D; X.sup.3 is selected from amino acids R, V, P; X.sup.4 is selected from amino acids V, L, S; X.sup.5 is selected from amino acids T, G, R; X.sup.6 is selected from amino acids G, T; X.sup.7 is selected from amino acids L, A; X.sup.8 is selected from amino acids V, I; X.sup.9 is selected from amino acids G, A, R; X.sup.10 is selected from amino acids R, A, G;
with a directly attached alpha-helical structure at the N-terminus or C-terminus is disclosed.

In one aspect, provided herein are recombinant neuraminidases comprising an ectodomain of influenza virus neuraminidase with amino acid substitutions or insertions of cysteines in the stalk domain to generate a more stable, tetrameric influenza virus neuraminidase. In specific embodiments, the influenza virus neuraminidase further comprises influenza virus neuraminidase transmembrane and cytoplasmic domains. In another aspect, provided herein are recombinant neuraminidase comprising a globular head domain of influenza virus neuraminidase and a tetramerization domain, wherein the recombinant neuraminidase lacks influenza virus neuraminidase stalk, transmembrane and cytoplasmic domains. In another aspect, provided herein are methods of immunizing against influenza virus using such recombinant neuraminidases or compositions thereof.

The present disclosure relates to, inter alia, a weed control method. In one example, a method comprises applying to the locus a weed controlling amount of a pesticide composition comprising a FatA acyl-ACP thioesterase-inhibiting herbicide, wherein the crop plants are modified such that they comprise a FatA acyl-ACP thioesterase which provides the crop plant with tolerance against the FatA acyl-ACP thioesterase-inhibiting herbicide. Recombinant polynucleotides and suitable for use in the methods, and edited FatA acyl-ACP thioesterases are also disclosed.

Mussels strongly adhere to a variety of surfaces by secreting byssal threads that contain mussel foot proteins (Mfps). Recombinant production of Mfps presents an attractive route for preparing advanced adhesive materials. Using synthetic biology strategies, Mfp5 together with Mfp5 oligomers containing two or three consecutive, covalently-linked Mfp5 sequences (named Mfp5.sup.2 and Mfp5.sup.3) were synthesized. Positive correlations were found between Mfp5 molecular weight and underwater adhesive properties, including adhesion force, adhesion work, protein layer thickness, and recovery distance. Dopa-modified Mfp5.sup.3 displayed a high adhesion force (201±36 nN μm.sup.−1) and a high adhesion work (68±21 fJ μm.sup.−1) for 200 s cure times, higher than previously reported Mfp-mimetic adhesives. Results disclosed herein highlight the power of synthetic biology in producing biocompatible and highly adhesive Mfp-based materials.