Provided is a supramolecular polypeptide comprising alternating repeats of crystallite-forming subsequences and amorphous subsequences. The crystallite-forming subsequences form crystallites comprising stacks of one or more β-sheets and the amorphous subsequences form a network of hydrogen bonds. The supramolecular polypeptides are capable of exhibiting self-healing behavior.

Cell-targeted cytotoxic agents, including sortase serine protease constructs, are provided. Such compounds can be used in methods for targeted cell killing such as for treatment cell of proliferative diseases (e.g., cancer). In some aspects, recombinant sortase serine proteases, such as Granzyme B polypeptides, are provided that exhibit improved stability and cell toxicity.

The present invention relates to a method for preparing a protein cage which comprises: a 1.sup.st step of preparing an amphiphilic polymer comprising a 1.sup.st hydrophobic polymer and a 1.sup.st hydrophilic functional group; a 2.sup.nd step of preparing a hydrophilic protein comprising a 2.sup.nd functional group binding to the 1.sup.st functional group; a 3.sup.rd step of forming an amphiphilic polymer-protein hybrid by the binding of the 1.sup.st functional group and the 2.sup.nd functional group, and forming core-shell structured particles comprising a protein shell and an amphiphilic polymer core by the self-assembly of the amphiphilic polymer in a hydrophilic solvent; and a fourth step of removing some or all of the hydrophobic polymer of the core part from the core-shell structured particles.

A method of quantifying expression of a protein of interest with high temporal resolution; it includes providing a cell expressing a large fragment of a split fluorescent protein; transfecting the cell with a vector comprising a nucleic acid molecule comprising a first nucleic acid sequence encoding the protein of interest; a second nucleic acid sequence encoding the small fragment of the split fluorescent protein; and a third nucleic acid sequence encoding a linker protein that is cleaved during translation; quantifying expression of the protein of interest by detecting fluorescence resulting from a combining of the small fragment of the split fluorescent protein and the large fragment of the split fluorescent protein, wherein the linker protein is cleaved during the translation resulting in a stoichiometric ratio of the small fragment of the split fluorescent protein and the protein of interest.

The present invention provides a tool which exhibits excellent properties in the quantification of autophagy activity. A unimolecular FRET probe of the present invention includes an acceptor consisting of a fluorescent protein to be enzymatically degraded inside a lysosome or a vacuole; and a donor having an amino acid sequence having a sequence identity of 95% or more with respect to an amino acid sequence represented by SEQ ID NO: 1.

The present invention relates to the field of genetic engineering, particularly to a recombinant expression vector for rapidly screening the high expression strains and a method for rapidly screening high expression strains. In the invention, an exogenous red fluorescent protein and Aspergillus fumigatus cell surface protein localization signal are fused and expressed, and the fusion gene (DsRed-AfMP1) is integrated into the genome of Trichoderma reesei, so as to construct a strain displaying red fluorescent protein on the surface of Trichoderma reesei. By sorting Trichoderma reesei strains with red fluorescent protein on the surface by flow cytometry, genes beneficial to the improvement of cellulase activity can be quickly isolated.

The present invention is directed generally to cell-targeted cytotoxic constructs comprising a targeting polypeptide, a linking polypeptide and a cytotoxic polypeptide. Preferably, (a) the targeting polypeptide is a R-spondin1 (RSPO1), R-spondin2 (RSPO2) or yoked chorionic gonadotropin (YCG), the linking polypeptide comprises LPXT (SEQ ID NO: 56) or NPXT (SEQ ID NO: 60) as well as others, where X is any amino acid, the linking polypeptide being positioned between the targeting ligand and (c) the cytotoxic moiety is an auristatin or a truncated serine protease, the serine protease having an IIGG (SEQ ID NO: 91), IVGG (SEQ ID NO: 92) or ILGG (SEQ ID NO: 93) at its N-terminus. Such constructs can be used in methods for targeted cell killing such as for treatment cell of proliferative diseases (e.g., cancer).

A composition includes aluminum hydroxide gel and a conjugate of at least one CysA13(33-40) peptide linked to the keyhole limpet hemocyanin (KLH). Maleimidobutyric acid Nhydroxysuccinimide ester (SM) serves as cross-linking agent. The composition can produce an effective and specific immune response against Aβ40. The antibodies produced are specific for Aβ40 without significantly binding to Aβ42. The composition can increase the response against Aβ40 compared with the response produced by other conjugates that include CysAβ(33-40) peptide and KLH, and are bound or conjugated by other crosslinking agents.

55139597

Non-human animals and methods and compositions for making and using them are provided, wherein said non-human animals have a genome comprising an engineered or recombinant diversity cluster within an immunoglobulin heavy chain variable region, which engineered or recombinant diversity cluster comprises an insertion of one or more coding sequences of a non-immunoglobulin polypeptide of interest. Non-human animals described herein express antibodies characterized by complementary determining regions (CDRs), in particular, CDR3s having diversity that directs binding to particular antigens. Methods for producing antibodies from non-human animals are also provided, which antibodies contain human variable regions and mouse constant regions.

Disclosed is a mussel adhesive protein including at least one photocaged 3,4-dihydroxyphenylalanine derivative residue including a protecting group on at least one hydroxyl residue of its catechol moiety. The photocaged 3,4-dihydroxyphenylalanine derivative residue replaces a naturally occurring amino acid and the protecting group can be cleaved from the 3,4-dihydroxyphenylalanine derivative residue by irradiation with UV light.