15 results about "Protein dimer" patented technology

The invention relates to an islet repair ICK mode oral polypeptide optimization system taking VDAC1 as a target based on ESM2 and a genetic algorithm, and the system comprises a mutation module which is used for carrying out mutation and recombination by adopting the genetic algorithm according to original protein sequence data to generate an initial population; the prediction module is used for respectively inputting the protein sequence data of the initial population into a protein dimer dissociation energy prediction model, a protein toxicity prediction model and a protein cell penetrability prediction model to obtain a dissociation energy prediction value delta G, a toxicity probability value T and a cell membrane passing transmission probability Ed; and the optimization module is used for acquiring the optimal individual performance of the highest fitness score to output the Pareto optimal sequence index, and recording the hotspot residue distribution and the site mutation frequency at the same time. On the basis of keeping the biological activity of the original sequence, the key drug properties are improved in a breakthrough manner.

Disclosed are a new interleukin-2 (IL-2) mutant protein and the use thereof. Compared with wild-type IL-2, the IL-2 mutant protein has improved properties, such as an improved IL-2 receptor binding property and improved druggability. Also provided are a fusion protein, dimer and immunoconjugate comprising the IL-2 mutant protein, nucleic acids encoding the IL-2 mutant protein, the dimer and the immunoconjugate, and a vector and host cell comprising the nucleic acid. Further provided are methods for preparing the IL-2 mutant protein, the fusion protein, the dimer and the immunoconjugate, a pharmaceutical composition containing same, and the therapeutic use thereof.

Bispecific antibodies comprising mutations that decrease homodimerization and at least one immunogenic peptide inserted into a CHI or CL domain are provided. Proteins comprising an Fc variant of a parent Fc polypeptide wherein at least one immunogenic peptide is inserted into the parent Fc polypeptide and the insertion replaces amino acids of the parent Fc polypeptide are provided. Protein dimers and antibodies comprising the proteins of the invention are also provided as are nucleic acid molecules encoding same, pharmaceutical compositions comprising same and methods of treating cancer by administrating same. Methods of producing antibodies are also provided.

The invention relates to the field of antibody proteins, in particular to an immunoglobulin Fc dimer with a stable disulfide bond, an Fc fusion protein containing the Fc protein dimer and a calculation design method of the Fc fusion protein. The immunoglobulin Fc protein dimer comprises two protein subunits, a CH3 structural domain of each subunit contains at least one cysteine mutation, and the two protein subunits are combined through an interchain disulfide bond formed by mutation cysteine. Cysteine mutation is specifically introduced into the CH3 structural domain of the Fc region of the immunoglobulin to form a stable interchain disulfide bond, so that the problem of insufficient stability of the Fc protein dimer is solved.

The present invention relates to aptamers that specifically bind to the extra-cellular domain of alpha7 / beta1 integrin dimers, conjugates or particles comprising said aptamers, in muscles cells such as skeletal muscle fibres and satellite cells, or in cells aberrantly expressing said domain e.g. tumour cells such as rhabdomyosarcoma (muscle-derived tumours), or glioblastoma cancer stem cells, as well as conjugates comprising said aptamers, therapeutic or diagnostic compositions comprising said conjugates or said aptamers, and their use as a medicament and in diagnostic methods.

The application discloses a kind of MS2 virus-like particles based on capsid protein site-directed mutation and its preparation method and application, belong to molecular biological technique field.The amino acid of the beta sheet interface of capsid protein sequence, the amino acid of the interface when two capsid proteins molecules assemble, the carboxyl end site of capsid protein is subjected to site-directed mutation, obtain the mutant that can significantly improve the assembly efficiency and stability of capsid protein dimer.Utilize the mutant to construct MS2 virus-like particles, further by the design of mature enzyme and capsid protein expression element, control mature enzyme weak expression, capsid protein strong expression, to improve assembly efficiency.The application improves the assembly efficiency of MS2 virus by the above strategy, improves the proportion of wrapped RNA, enhances the stability of virus-like particle, greatly prolongs the stable storage time of RNA, improves the purity of wrapped RNA.

The invention discloses a natural neutrophil apolipoprotein dimer and a preparation method thereof, and belongs to the technical field of biomolecule preparation and biomedical detection. The problems that the recombinant protein dimer prepared by a genetic engineering recombination technology is low in yield, the structure of the recombinant protein dimer is different from that of natural protein, so that the development of antibodies and the detection effect of related kits are influenced, a method for extracting the recombinant protein dimer from peripheral blood is complicated, raw materials are not easy to obtain, and blood resources are wasted are solved. According to the preparation method disclosed by the invention, a leukocyte filter or a leukocyte layer generated in a component blood preparation process is taken as a raw material, a leukocyte lysis solution is adopted for lysis, and the obtained granulocyte lysis solution is combined with anion exchange and affinity chromatography methods to obtain the natural neutrophil apolipoprotein dimer. The preparation method can be used for preparing the natural neutrophil apolipoprotein dimer in batches, is simple and convenient to operate and high in protein yield, and can realize comprehensive utilization of blood resources and turn waste into wealth.

This invention provides a multi-site mutant of cocaine esterase, its protein dimer, and its applications. By mutating cysteine ​​(C) at position 107 to serine (S), and cysteine ​​(C) at position 551 to serine (S), arginine (R), or alanine (A), it achieves efficient and uniform cross-linking with BMOE while maintaining cocaine catalytic activity, forming a structurally stable dimer. This modification significantly improves the enzyme's thermostability and prolongs its half-life in vivo. The protein dimer is suitable for the treatment and prevention of acute cocaine poisoning.

The present application relates to a protein dimer formed from a first fusion protein and a second fusion protein, wherein the first fusion protein comprises a cystine knot domain (CK) fused to a first pharmaceutically active protein and the second fusion protein comprises a CK domain fused to a second pharmaceutically active protein, wherein the two fusion proteins are covalently linked via their CK domains. The present application further relates to the individual fusion proteins, polynucleotides encoding the fusion proteins, vectors comprising the polynucleotides, and host cells comprising the vectors.

The present application relates to a novel coronavirus RBD fusion protein, an RBD protein dimer and a preparation method and application thereof for preventing novel coronavirus SARS-CoV-2 infection.

The problem addressed by the present invention is to produce a novel antibody recognizing a mutant CALR protein at a site distinct from the sites recognized by conventional antibodies, and to provide pharmaceuticals using the same. The present invention provides a composition for treating a tumor, the composition comprising an antibody or an antigen-binding fragment thereof that binds to a region N-terminal to a mutation site in a mutant calreticulin and binds to the mutant calreticulin present on the cell surface. The present invention also provides a method for producing an antibody that binds to a region N-terminal to a mutation site in a mutant calreticulin, said method comprising a step for screening: an antibody that binds to the mutant calreticulin present on a cell surface; or an antibody that binds to a dimer of the mutant calreticulin.

The application discloses a purification method of recombinant human bone morphogenetic protein-2 dimers. The purification method comprises the following steps: S1, carrying out affinity capture on the denatured recombinant human bone morphogenetic protein-2 inclusion body, and then adopting a renaturation liquid to perform on-column linear gradient renaturation; S2, adopting an arginine-containing buffer to elute the affinity chromatography column after S1 treatment, dropping the eluted protein liquid into an incubation buffer to perform incubation, and obtaining a protein mixture; S3, performing cation chromatography on the protein mixture, and adopting buffers containing different concentrations of arginine to flush the cation chromatography column, so that the recombinant human bone morphogenetic protein-2 dimers are obtained. The recombinant human bone morphogenetic protein-2 dimers are purified by the method, the process connection is reasonable, the production cycle is short, the obtained protein has high yield and low cost, the process is stable, and the method is very suitable for large-scale commercial production; meanwhile, the purification process also provides a reference for the research and production of similar recombinant protein drugs.

This invention belongs to the field of pharmaceutical technology and discloses the inhibitory effects and mechanisms of action of sclerotinib on lung cancer cells, cervical cancer cells, and ovarian cancer cells. Compared with the currently available broad-spectrum antitumor drug fluorouracil, sclerotinib exhibits superior antitumor properties. In-depth research revealed that sclerotinib acts on the novel protein STAT3 in cancer treatment, inhibiting STAT3 phosphorylation and preventing phosphonate-modified protein dimers from entering the cell nucleus to initiate transcription. Furthermore, sclerotinib inhibits the downstream anti-apoptotic protein BCL-2 of STAT3, synergistically inhibiting tumor cell proliferation. In this study, based on the half-maximal inhibitory concentration (IC50) results of sclerotinib against lung cancer cells A549, cervical cancer cells HeLa, and ovarian cancer cells A2780, we directly verified the anticancer target of sclerotinib through experiments, elucidated its anticancer mechanism, and provided theoretical and experimental basis for its entry into preclinical and clinical trials.

Compositions comprising nanoparticles comprising albumin and rapamycin, and commercial batches of such compositions are provided.SOLUTION: A nanoparticle composition comprising (a) nanoparticles comprising rapamycin and albumin and (b) a non-nanoparticle portion comprising albumin and rapamycin, wherein about 80% to about 95% of the albumin in the composition is in the form of monomeric albumin and about 4% to about 15% of the albumin in the composition is in the form of dimeric albumin, as measured by subjecting the composition to size exclusion chromatography (SEC) with a saline mobile phase coupled with a multi-angle light scattering (MALS) detector, wherein the percentage of albumin in the composition that is in the form of monomeric albumin, dimeric albumin or polymeric albumin is determined by: And wherein about 0.5% to about 5% of the albumin in the composition is in the form of polymeric albumin.SELECTED DRAWING: Figure 11

This invention provides a fusion protein dimer comprising a dimer of a first dimerizing polypeptide and a second dimerizing polypeptide, wherein (a) the first dimerizing polypeptide is attached by a peptide bond or via a peptide linker at its N-terminus or C-terminus to a first domain, and the second dimerizing polypeptide is attached by a peptide bond or via a peptide linker at its N-terminus or C-terminus to a second domain, (b) the first and second dimerizing polypeptides comprise amino acids 616 to 726 of ACE2, (c) the first dimerizing polypeptide is optionally attached by a peptide bond or via a peptide linker at its remaining free N-terminus or C-terminus to a third domain, and (d) the second dimerizing polypeptide is optionally attached by a peptide bond or via a peptide linker at its remaining free N-terminus or C-terminus to a fourth domain.