57 results about "Amino terminal" patented technology

A system for delivering a payload nucleic acid into target cells of a subject and production of a payload (or payloads) encoded by the payload nucleic acid in the cells. The system includes a Bifidobacterium sp. bacterium comprising a plasmid and a transporter nucleic acid, the transporter nucleic acid configured for expression in the bacterium. The transporter nucleic acid encodes a transporter polypeptide comprising, in an amino-terminal to carboxy-terminal order, a bacterial secretion signal peptide, a DNA-binding domain to bind the plasmid, and a cell penetrating peptide. The transporter polypeptide complexes with the plasmid and transports the plasmid from the bacterium into the target cells. The plasmid encodes one or more payloads (protein and / or ribonucleic acid) for production in the target cells. The target cells may be colonic cells. When the payload(s) include an antigen, the system may be a DNA vaccine.

The invention relates to the technical field of single-molecule devices, in particular to a single-molecule device for detecting small-molecule gas based on supramolecules and a preparation method of the single-molecule device. The monomolecular device comprises a functional molecule and a graphene electrode pair, wherein the functional molecule is connected between the graphene electrode pair through an amido bond. A cucurbituril hydrophobic cavity structure in the functional molecular structural formula can contain and capture target small molecular gas, gas molecules of different volumes are selectively included through multiple weak interaction, a dynamically-adjustable subject-object compound structure is formed, and then switching type sensing detection on the small molecular gas is achieved. The amino terminal of the end part of the main bridging unit in the functional molecule can be connected with the carboxyl terminal of the graphene point electrode in a covalent bond manner, and amide condensation molecular chain connection is formed at the two ends of the graphene point electrode, so that the stability of a monomolecular device is improved. The preparation method provided by the invention is simple in process, mild and controllable in reaction condition and beneficial to large-scale production.

The invention discloses decapeptide with antioxidant activity, the amino acid sequence of the decapeptide is amino terminal-APKTLPWGPK-carboxyl terminal, and the decapeptide can be developed into an antioxidant.

The present application relates to a milk-derived phosphorylated peptide with the activity of improving intestinal iron absorption and its application in the preparation of iron supplements. The sequence of the milk-derived phosphorylated peptide is EESITRINKKIE, and the glutamic acid at the amino terminal of the sequence is connected with 1-3 phosphoserines. The milk-derived phosphorylated peptide can be combined with Fe 2+ Specifically bound, strong iron chelating ability, and can significantly improve the iron transport amount in the Caco-2 small intestinal epithelial cell model, thereby having good activity of improving intestinal iron absorption, and can be widely applied in the fields of drugs, health care products or food.

The application belongs to the technical field of biological detection, and discloses a cardiovascular marker control article and a preparation method thereof. The cardiovascular marker control article comprises a serum matrix, antigens, a preservative and a stabilizer. The antigens include cardiac troponin I antigens, creatine kinase isoenzyme antigens, myoglobin antigens, amino-terminal brain natriuretic peptide precursor antigens, brain natriuretic peptide antigens, D-dimer antigens, heart-type fatty acid-binding protein antigens, myeloperoxidase antigens and lipoprotein phospholipase A2 antigens. The stabilizer includes at least one of D-trehalose, sucrose, glycine, inositol and polyethylene glycol. The cardiovascular marker control article can cover various cardiovascular disease markers, including heart failure, pulmonary embolism, vasculitis and atherosclerosis, myocardial injury, myocardial infarction and the like. The control article can be used as a third-party control article for indoor and inter-laboratory quality control of a cardiovascular disease screening and auxiliary diagnosis measurement system.

The present disclosure relates generally to transposase domains, in particular transposase domains comprising an amino terminal deletion, as well as transposase domains that form obligate heterodimers and transposase domains comprising a DNA targeting domain.

The invention provides amino resin as well as a preparation method and application thereof in the preparation process of allyl glycidyl ether. The amino resin comprises a styrene skeleton and an amino terminal, chloromethylated polystyrene is swelled and then reacts with an amine compound, the amino resin is used for replacing alkali liquor to serve as an acid-binding agent for a ring-closure reaction of an allyl alcohol chlorohydrin ether intermediate in the preparation process of allyl glycidyl ether, chlorine salt is not generated, and the reaction time is shortened. The three-waste treatment cost is greatly reduced, and meanwhile, the prepared amino resin can be regenerated through heating and can be repeatedly used.

Activatable interleukin 12 (IL12) fusion proteins and constructs are disclosed herein that contain at least one of the following structures: N'-DD-L1-MM-L2-IL12-C', C'-DD-L1-MM-L2-IL12-N', N'-DD-L1-IL12-L2-MM-C', C'-DD-L1-IL12-L2-MM-N', wherein L1 is a first linker or is absent; L2 is a second linker; DD is a dimerization domain; MM is a masking moiety; IL12 comprises an IL12α (p35) domain and an IL12β (p40) domain; N' is an amino terminus of the activatable IL12 fusion protein; and C' is a carboxy terminus of the activatable IL12 fusion protein, wherein at least one of L1 and L2 comprises a cleavable moiety (CM); or a first IL12 subunit and a second IL12 subunit; at least one of a first linking region (LR1) and a second linking region (LR2); and a half-life extending moiety (EM), wherein at least one of the LR1 and the LR2 comprises a cleavable moiety (CM); or dimers thereof.

The application discloses a method for conformational signal peptide-mediated secretion and expression of heterologous proteins in Escherichia coli, and specifically comprises the following steps: simultaneously fusing at least two heterologous proteins to a conformational signal peptide (such as sfGFP) and constructing a heterologous recombinant protein expression vector, wherein the conformational signal peptide has a beta-barrel structure, and the fusion sites are at least two of the amino terminal end, the carboxyl terminal end and a plurality of loop rings of the conformational signal peptide; and then transforming the heterologous recombinant protein expression vector into Escherichia coli and culturing the obtained genetic engineering strain for expression. According to the method, the extracellular secretion and expression of the heterologous proteins in the Escherichia coli can be realized without the mediation of a classical signal peptide, the sfGFP as a fusion tag has no influence on the function of the target protein, and the corresponding target protein can be quickly expressed and purified; and the method expands the secretion and expression path of the protein, can realize the simultaneous expression of a plurality of heterologous proteins, and can effectively improve the expression amount of the target protein.

The BTK-C isoform is expressed in human breast and prostate cancer cells and it plays a crucial role in epithelial cancer cell survival. BTK-C has a 34 amino acid extension to the n-terminus that facilitate it being palmitoylated on two cysteine residues. This modification localizes BTK-C closer to the cell membrane where it plays a role in improving cancer cell survival, as compared to BTK-A. BTK-C is not found to be expressed in healthy adult cells, whereas BTK-A is necessary for immune cell production. Disclosed herein are alternative kinases besides BTK having similar attributes, which present therapeutic opportunities for the treatment of cancers, especially for solid tumors.

The invention provides a whey protein isolate source antioxidant polypeptide, the amino acid sequence of the whey protein isolate source antioxidant polypeptide is amino terminal-LVYPFPGPIP-carboxyl terminal, and the whey protein isolate source antioxidant polypeptide can be developed into an antioxidant.

The present disclosure relates to bispecific binding proteins comprising, from the amino terminal to the carboxy terminal, (a) a first moiety, which is an anti-BAFF antibody or antigen binding fragment thereof, and (b) a second moiety, which is an anti-MASP2scFv or truncated TACI polypeptide. Furthermore, the invention relates to nucleic acid molecules encoding such bispecific binding proteins, as well as vectors and host cells comprising such nucleic acid molecules. The invention further relates to a method for producing said bispecific binding proteins and to the use of said bispecific binding proteins in the treatment of autoimmune diseases.

This disclosure generally relates to fusion proteins comprising TAL Arrays targeting a repetitive element and a transposase domain comprising amino terminal deletions, as well as dual cysteine rich domains (CRD), for targeting site-specific transposition into ribosomal DNA (rDNA) repeats or LINE1 repetitive elements, polynucleotides and vectors encoding the fusion proteins, and methods of use therefor.

The present application belongs to the technical field of organic framework materials, and particularly relates to a kind of covalent organic framework material and its preparation method and application.The present application covalent organic framework material includes electron donor and electron acceptor;Electron donor and electron acceptor are connected by covalent bond;Electron donor includes organic ligand containing aldehyde group terminal group;Electron acceptor includes organic ligand containing amino terminal group.The present application is constructed by specific kind of electron donor-electron acceptor structure, so that the redox center in the covalent organic framework material is separated in space, which is beneficial to the rapid separation and migration of photo-generated carriers and improves the lifetime of photo-generated carriers, thereby efficient photocatalysis-piezoelectricity synergistic catalytic reaction is generated H2O2, and the yield of hydrogen peroxide can be obviously improved, and under the synergistic effect of photocatalysis-piezoelectricity, the efficiency of hydrogen peroxide produced by the material is higher than that under the condition of photocatalysis.

The invention discloses a method for preparing semeglutide by using a natural chemical ligation method, which comprises the following steps: (1) synthesizing semeglutide in two segments, namely an N-terminal segment with carboxyl-terminal hydrazide and a C-terminal segment with amino-terminal cysteine; (2) connecting the two fragments through a natural chemical connection method under a buffer salt condition; and (3) performing desulfurization treatment to convert Cys into target amino acid, and performing purification and freeze-drying after complete treatment. According to the method, the semeglutide is divided into the C-terminal polypeptide fragment and the N-terminal polypeptide fragment, the C-terminal polypeptide fragment and the N-terminal polypeptide fragment are connected through natural chemical connection reaction after being prepared respectively, then desulfurization treatment is conducted, the high-purity and high-yield semeglutide is finally obtained, the problem of difficult sequences is solved, the synthesis efficiency and purity of the semeglutide are remarkably improved, and the method is suitable for industrial production. The method is suitable for large-scale production.

The invention discloses a whey protein source peptide with hyaluronidase inhibitory activity. The whey protein source peptide is characterized in that the sequence of the whey protein source peptide is amino terminal-GGVSLPEW-carboxyl terminal. The peptide has the advantages of no toxicity, no sensitization and the like, has a remarkable inhibition effect on hyaluronidase, and can be used for developing functional foods or medicines with anti-allergic characteristics.

The invention provides a biosensor for detecting nitrate content as well as a preparation method and application thereof, and relates to the technical field of biology. The biosensor disclosed by the invention comprises a luciferase amino terminal fragment, a luciferase carboxyl terminal fragment and NasR protein, the luciferase amino terminal fragment and the luciferase carboxyl terminal fragment are two fragments of the same luciferase. The biosensor provided by the invention has high selectivity on nitrate, can specifically, stably, continuously and online observe the nitrate content in the whole plant for a long time, and overcomes the key problems of destructive sampling, limited spatial resolution, insufficient detection sensitivity and the like in the traditional method; and a real-time dynamic detection platform capable of monitoring the whole plant living body is provided for plant nitrogen metabolism research.

The present invention relates to the biomedical and biopharmaceutical sectors. Specifically, it relates to a chimeric antigen comprising the combination of the amino- and carboxy-terminal regions of the amyloid-beta peptide (Aβ), the amino- and carboxy-terminal regions of the tau protein, and a T-cell epitope. The pharmaceutical composition comprising this chimeric antigen and at least one pharmaceutically acceptable vaccine adjuvant increases the efficacy of immunotherapy for the prevention and treatment of Alzheimer's disease (AD). The chimeric antigen exerts its action by stimulating a multi-target humoral response with high titers of anti-Aβ and anti-tau antibodies simultaneously. This promotes the combined elimination of toxic Aβ and tau species from the brain, thereby preventing or significantly improving the clinical symptoms and neuropathology of AD.

To provide an antitumor antagonist comprising a first targeting domain comprising a mutated TGFβ1-R11 extracellular domain (mutated ECD); and an immunoglobulin scaffold having an amino terminus and a carboxy terminus.SOLUTION: The present disclosure relates to an antitumor antagonist comprising a first targeting domain comprising a mutated TGFβ1-R11 extracellular domain (mutated ECD); and an immunoglobulin scaffold having an amino terminus and a carboxy terminus, the one or more mutations reducing proteolytic cleavage of the antitumor antagonist. Also disclosed are methods for treating proliferative disorders, infections, and immunological disorders with the antitumor antagonists described herein.SELECTED DRAWING: Figure 20

The application provides a preparation method of dopamine (DA) modified polyamide-amine dendrimer, which comprises amino terminal dopamine carboxylation, synthesis of carboxylated dopamine with a protective group, synthesis of carboxylated dopamine with a protective group modified polyamide-amine dendrimer, and synthesis and application of dopamine modified polyamide-amine dendrimer. The application utilizes the firm adhesion performance of DA in a marine humid environment, the antibacterial performance and the osteogenic induction performance of PAMAM-NH2 cationic polymer, introduces DA into the surface of PAMAM-NH2 to synthesize a new high polymer material DA-PAMAM-NH2, detects the long-acting antibacterial and osteogenic induction performance of the system as a bifunctional coating on the surface of an implant, and evaluates the role of the system in improving the clinical durability of the implant.

The invention discloses a whey protein source peptide with hyaluronidase inhibitory activity. The whey protein source peptide is characterized in that the sequence of the whey protein source peptide is amino terminal-GVSLPEW-carboxyl terminal. The peptide has the advantages of no toxicity, no sensitization and the like, has a remarkable inhibition effect on hyaluronidase, and can be used for developing functional foods or medicines with anti-allergic characteristics.

Compositions and methods relating to paraoxonase fusion polypeptides are disclosed. In some aspects, the fusions are bispecific molecules that include a first biologically active polypeptide linked amino-terminal to a biologically active paraoxonase, wherein the first biologically active polypeptide is a DNase, an RNase, a SOD1, a CTLA-4 extracellular domain, a CD40 extracellular domain, or a polypeptide that specifically binds and neutralizes an inflammatory cytokine. Bispecific fusions may further include a second biologically active polypeptide (e.g., a dimerizing or FcRn-binding domain) linked carboxyl-terminal to the first biologically active polypeptide and amino-terminal to the paraoxonase. In other aspects, a fusion polypeptide includes a biologically active paraoxonase linked carboxyl-terminal or amino-terminal to a dimerizing or FcRn-binding domain. Also disclosed are dimeric proteins comprising first and second paraoxonase fusion polypeptides as disclosed herein. The fusion polypeptides and dimeric proteins are useful in methods for therapy.

The present invention relates to a fusion peptide, a salt thereof, or a solvate thereof, the fusion peptide containing, from the amino terminus toward the carboxy terminus, a tag peptide and any peptide among (A1)-(A3). (A1) A peptide that comprises the amino acid sequence represented by SEQ ID NO: 1; (A2) a peptide that comprises an amino acid sequence obtained by deleting, substituting, or adding 1-4 amino acids in the amino acid sequence represented by SEQ ID NO: 1 and that has a pore density increasing effect; and (A3) a peptide that comprises an amino acid sequence having 90% or more sequence identity with the amino acid sequence represented by SEQ ID NO: 1 and that has a pore density increasing effect.

The present application belongs to the technical field of protein engineering and genetic engineering, and particularly relates to a recombinant collagen XVII and a preparation method and application thereof. Specifically, a brand new recombinant collagen is designed through screening, replacement and splicing, the nucleotide sequence of the recombinant collagen is optimized according to the codon bias of Pichia pastoris, a transmembrane peptide is introduced into the amino terminal of the sequence, a corresponding genetic engineering yeast strain is constructed, and the recombinant collagen is successfully prepared through fermentation. The amino acid sequence of the recombinant collagen has a homology of 100% with the corresponding region of natural human collagen XVII, and there is no immunogenicity risk caused by sequence difference. Meanwhile, the endotoxin content of the protein can be controlled through a purification process, so that no endotoxin residue is ensured. The recombinant collagen prepared by the above technical scheme has more excellent transdermal performance and cell proliferation activity, and has better stability, and therefore has good practical application value.

The invention belongs to the technical field of protein engineering and genetic engineering, and particularly relates to a recombinant XVII type collagen as well as a preparation method and application thereof. Specifically, brand new recombinant collagen is designed by means of screening, replacement, splicing and the like, pichia pastoris codon preference optimization is performed on a nucleotide sequence of the recombinant collagen, cell-penetrating peptide is introduced to an amino terminal of the sequence, a corresponding genetic engineering yeast strain is constructed and obtained, and the recombinant collagen is successfully prepared by fermentation. The homology of the amino acid sequence of the gene and the corresponding region of the natural human source XVII type collagen reaches 100%, and the immunogenicity risk caused by sequence difference does not exist; meanwhile, the endotoxin content of the protein can be controlled through a purification process, and no endotoxin residue is ensured. The recombinant collagen prepared by the technical scheme has more excellent transdermal performance and cell proliferation activity, and also has better stability, so that the recombinant collagen has good practical application value.

By deleting a nucleotide sequence encoding the amino terminal region and a nucleotide sequence encoding the carboxy terminal region of the E120R protein in the genome, the modified African swine fever virus does not remain in the body of the inoculated animal and exhibits a vaccine effect against African swine fever.

A preparation method for and use of a scopoletin-functionalized magnetic nanoprobe. The preparation method comprises steps such as preparation of amino-terminal modified nanoparticles Fe3O4@SiO2-NH2, preparation of a photoaffinity linker-scopoletin conjugate, preparation of the scopoletin-functionalized magnetic nanoprobe, etc. The method features simple and rapid operation, and eliminates the need for prior clarification of the structure-activity relationship of the active compounds, without compromising all-round contact between the active compounds and target proteins. The prepared scopoletin-functionalized magnetic nanoprobe is used for target fishing in cellular and animal models of rheumatoid arthritis. After the captured target proteins are isolated and subjected to mass spectrometry identification, a western blot experiment successfully verifies vimentin as the target protein of scopoletin on HFLS-RA cell membranes, thereby providing a novel therapeutic target for rheumatoid arthritis.

The present invention provides a carrier for biological treatment, which enables sludge to adhere easily through the carrier for biological treatment and has a high ability to purify waste water, and which is characterized in that the carrier for biological treatment is composed of nylon fibers, the number of amino terminal groups, which are the polymer properties of the nylon fibers, is 40 [mu] eq / g or more, and the molar fraction FA of the amino terminal groups is 0.45 or more. The relative viscosity [eta] r of the polymer of the nylon fiber is 2.5 or more.

The invention provides single-molecular-weight oligoproline with thermal responsiveness as well as a preparation method and application thereof, and belongs to the technical field of biological materials and high polymer chemistry. The preparation method comprises the following steps: synthesizing an oligoproline-solid-phase carrier compound with a protected amino terminal by adopting a solid-phase synthesis method; after an amino terminal protecting group is removed, carboxylic acid containing a hydrophobic group reacts with the amino terminal protecting group to realize hydrophobic modification of the amino terminal; and finally, cutting and purifying to obtain the thermal-responsive single-molecular-weight oligomeric proline of which the amino terminal is modified by a hydrophobic group. According to the invention, C2-C8 alkyl is introduced into the terminal amino group of oligoproline, so that oligoproline with low molecular weight and single molecular weight is successfully endowed with thermal responsiveness, the product structure is clear, the phase change behavior is clear, an ideal model is provided for design of a temperature-sensitive material and research on a phase separation mechanism, and the application prospect is wide. And the application of oligoproline in the fields of biological materials and drug delivery is expanded.

This disclosure relates to nanoparticles coated with fusion proteins comprising a domain that binds a cancer marker and a domain comprising a toxic polypeptide. In certain embodiments, the targeted cancer marker is urokinase plasminogen activator receptor (uPAR) insulin-like growth factor 1 receptor (IGF1R), EGFR, HER2, and / or other member of the ErbB family of receptors. In certain embodiments, the molecule that binds a cancer marker is an amino terminal fragment of uPA or variant capable of binding uPAR and / or IGF1 or variant capable of binding IGF1R. In certain embodiments, the toxic polypeptide is a bacterial exotoxin.