33 results about "Peptide bond" patented technology

This invention belongs to the field of photocrosslinking probe technology, specifically relating to a GUSB photocrosslinking probe, its preparation method, and its application. The GUSB photocrosslinking probe has the general chemical formula C0. 13 H 18 N2O6-R, wherein R is any one of the oxalic group elements or peptide bonds. The R group covalently connects the glucuronic acid recognition core and the photosensitive unit in the GUSB photocrosslinking probe, and the R group contains no more than 4 atoms, resulting in a small size and low steric hindrance. The GUSB photocrosslinking probe provided by this invention uses glucuronic acid as the recognition core, combined with a small-volume diazacyclopropane photosensitive unit and a terminal alkyne group, to achieve µM-level in-situ covalent capture of active GUSB in complex systems such as cells or tissues. The probe of this invention significantly improves positioning accuracy, sensitivity, data availability, quantification, and enrichment, while also possessing advantages such as modular synthesis, mild conditions, and strong system compatibility, effectively addressing the technical shortcomings of existing technologies that struggle to accurately obtain GUSB activity in situ under low-dose conditions.

This invention discloses a methanogenic lyase homologous to PeiR lyase and its applications. The PeiR lyase protein, targeting the peptide bonds of the methanogenic cell wall, participates in the biological process of hydrolyzing the archaea cell wall, effectively killing methanogens and reducing methane production. Proteins homologous to this lyase possess potential methane-reducing potential. This invention utilizes a series of bioinformatics software to identify protein sequences encoded by methanogenic viruses from a large amount of rumen microbial virome sequencing data, and analyzes the structural homology between these proteins and PeiR. Ultimately, this invention successfully obtained a series of methanogenic lyases homologous to PeiR. To achieve the expression of these lyases, this invention designed multiple primers to synthesize the target sequences and successfully expressed them in a prokaryotic expression system. In vitro gas production experiments with the crude enzyme solution showed that these lyases are effective in reducing methane production.

This invention provides a method for producing Clostridium neurotoxins containing an exogenous activation loop, modified Clostridium neurotoxins, and pharmaceutical compositions. [Solution] A method for proteolytically processing a single-chain Clostridium neurotoxin into a corresponding double-chain Clostridium neurotoxin, comprising: providing a single-chain Clostridium neurotoxin; and contacting the single-chain Clostridium neurotoxin with enterokinase or factor Xa, wherein the single-chain Clostridium neurotoxin has the polypeptide sequence Cys-(Xaa) a -Ile-Asp / Glu-Gly-Arg-(Yaa) b - A method in which an activation loop containing Cys (SEQ ID NO: 1) is present, a=1 to 10, b=4 to 15, and enterokinase or factor Xa hydrolyzes the peptide bond of the activation loop, thereby producing a double-stranded Clostridium neurotoxin.

The present disclosure provides a heterodimeric antibody, or antigen-binding fragment thereof, comprising two heavy chains with different amino acid sequences and a binding polypeptide. The heterodimer antibody, or the antigen-binding fragment thereof, include a first heavy chain comprising none or one or more modifications and the second heavy chain comprises one or more modifications and is fused to a binding polypeptide, which can form a isopeptide bond with a binding peptide. The present disclosure further provides systems and methods for purifying such heterodimeric antibodies, and antigen-binding fragments thereof.

This invention discloses a method for rapidly constructing a complex of cholera toxin B subunit (CTB) and antigen. The vaccine complex includes a CTB-SpyTag fusion protein and at least one SpyCatcher-antigen fusion protein. It also includes a preparation method for rapidly preparing a CTB5-antigen complex by mixing CTB-SpyTag with the SpyCatcher-antigen. This invention directs the antigen to the side of the CTB pentamer that does not participate in GM1 binding, avoiding steric hindrance interference. It utilizes the SpyTag / SpyCatcher covalent isopeptide bond to obtain highly stable antigen display, reducing antigen shedding during subsequent preparation and storage. It also possesses mucosal targeting and multivalent presentation functions, providing a universal platform technology for rapidly constructing and validating broad-spectrum, combined, or personalized mucosal vaccines.

This invention provides a recombinant Staphylococcus aureus enterotoxin B nanoparticle protein vaccine, mSEB-mi3, its preparation method, and its applications. This invention utilizes a SpyTag / SpyCather protein linker system to connect the recombinant protein to the nanoparticle protein, allowing mSEB to be displayed on the surface of self-contained nanoparticles, thus obtaining the recombinant Staphylococcus aureus enterotoxin B nanoparticle protein mSEB-mi3. Both mSEB-SpyTag and SpyCather-mi3 proteins in this invention are induced to be expressed in soluble form in Escherichia coli. The mSEB-SpyTag and SpyCather-mi3 of this invention can be covalently bound via isopeptide bonds to form the mSEB-mi3 nanoparticle protein vaccine. The binding conditions are simple, and when combined with the adjuvant MF59, it can induce rapid antibody production in mice, generating a high-level immune response and exerting a protective effect. Furthermore, its antibody response rate and protective efficiency are superior to those of the monomeric protein mSEB.

The present application aims to provide a novel peptide which shows a rapid effect of drug efficacy and potency and has a long relief maintenance period, a medicament and an external agent containing the same, and particularly a preventive or therapeutic agent for dermatitis, rough skin, rhinitis, alopecia, thin hair, a hair growth agent, a hair growth promoting agent, an antipruritic agent, a skin care product, and the like. The present application achieves the above aim by providing an amino acid sequence represented by Formula I, a cyclic peptide or a derivative thereof having no peptide bond other than between the amino acids constituting the amino acid sequence, or a pharmaceutically acceptable salt thereof.

The present application relates to a kind of tumor polypeptide vaccine. Specifically, the present application provides a kind of adjuvant-antigen peptide bond, and the adjuvant-antigen peptide bond is the structure shown in formula (I). The adjuvant-antigen peptide bond of the present application has excellent solubility, good drug property, and has excellent immune activation ability, can more effectively activate T cell, thereby play excellent immunotherapy effect, and has excellent treatment effect on tumor.

This invention provides a recombinant Staphylococcus aureus nanoparticle protein HI-mi3, its preparation method, and its applications. This protein is composed of HI (containing the key SA virulence factor α-hemolysin Hla). H35L The fusion protein HI and mi3 are composed of the N2 functional domain of the iron ion surface determinant B and self-assembled nanoparticle protein mi3. This invention uses the SpyTag / SpyCatCher protein coupling system to link the fusion protein antigen HI and mi3, obtaining the Staphylococcus aureus self-assembled nanoparticle protein HI-mi3. Both the recombinant protein SpyCatcher-mi3 and the recombinant protein SpyTag-HI of this invention are induced to be expressed in soluble form in Escherichia coli. The recombinant protein SpyCatcher-mi3 of this invention can covalently bind to the recombinant protein SpyTag-HI via isopeptide bonds to form the HI-mi3 nanoparticle vaccine molecule, with simple binding conditions. The HI-mi3 nanoparticle vaccine of this invention can induce a high level of immune response in animals and exert an immunoprotective effect.

The application discloses an algal protein peptide with anti-radiation activity and a preparation method and application thereof. The algal protein peptide is prepared by the following steps: adding pectinase and cellulase into red alga raw materials to release the algal protein by sol and lysis; adopting enzyme conversion to cut subunits to identify disulfide bonds and peptide bonds, so that a specific functional fragment component of the algal protein peptide is obtained; and through activity verification, the algal protein peptide with anti-radiation function is prepared in a targeted manner. The prepared algal protein peptide has a very strong protective effect on ultraviolet radiation HaCat cells, can effectively relieve cell DNA damage caused by UVB, improve cell survival rate under UVB irradiation, and reduce mortality. Therefore, the algal protein peptide can be applied to the preparation of food, cosmetics, drinks and other products, and has a good anti-radiation effect.

The application relates to the technical field of medical treatment and provides a CAR-gammadelta T cell targeting AXL and application thereof, the CAR-gammadelta T cell has a CAR molecule, the CAR molecule comprises the following structure: signal peptide-antiAXL scFv-extracellular hinge region-transmembrane region-co-stimulating factor-CD3 zeta intracellular region, the "-" is independently a connecting peptide or a peptide bond; the co-stimulating factor comprises a CD28 intracellular region and a 41BB intracellular region. Advantages: the CAR-gammadelta T cell targeting AXL integrates a third-generation CAR structure (CD28+4-1BB double co-stimulating domain) and a gammadelta T cell, realizes high targeting precision and killing efficiency. The in-vitro killing rate of the CAR-gammadelta T cell targeting AXL to AXL positive lung cancer cells (A549 and HCC827-ER3) is >90% (effector to target ratio 10:1), is obviously improved compared with common gammadelta T cells, and the tumor volume is obviously reduced in a PDX mouse model, which proves excellent treatment effect.

The present invention provides a compound having the structure: wherein A is a biologically active structure of the compound; wherein Z is a protein component of the compound, which protein component comprises one or more polypeptides, wherein at least one of the one or more polypeptides comprises consecutive amino acids which (i) are identical to a stretch of consecutive amino acids present in a chain of an Fc domain of an antibody; (ii) bind to an Fc receptor; and (iii) have at their N-terminus a sequence selected from the group consisting of a cysteine or selenocysteine; wherein the dashed line between B and Z represents a peptidyl linkage; and wherein the solid line between A and B represents a nonpeptidyl linkage, as well as intermediates dimers thereof, and processes of producing the compounds of the invention.

This invention relates to a genetically engineered bacterial outer membrane vesicle and its preparation method. By using in-cell peptides to attach exogenous proteins to the surface of OMVs via peptide bonds, a variety of desired antigens can be conveniently delivered. The reaction conditions are mild, less affected by antigen size, and unlike the SpyCatcher / SpyTag system, the in-cell peptides do not remain in the mature protein after attaching the exogenous protein to the OMV surface. This invention can serve as a universal tool for simultaneously or separately displaying different antigens on the surface of OMVs.

This invention discloses a method for removing beany odor substances from soybean protein based on sonochemical effects and synergistic protease-targeted enzymatic hydrolysis, belonging to the field of food processing technology. The method first integrates ultrasonic treatment into an "alkali dissolution and acid precipitation" process to prepare a soybean protein solution, which undergoes targeted enzymatic hydrolysis and vacuum degassing, and finally freeze-drying to obtain low-beany-odor soybean protein. This invention utilizes green, low-energy ultrasonic treatment, which effectively promotes protein structure unfolding through short-duration high shear and cavitation effects, exposing enzyme cleavage sites and increasing the contact opportunity between the substrate and the enzyme. Furthermore, by adding a complex protease to specifically hydrolyze the key peptide bonds binding soybean protein to beany odor substances, the dissociation and release of beany odor substances are promoted, achieving effective removal of the beany odor from the soybean protein.

The present disclosure provides a heterodimeric antibody, or antigen-binding fragment thereof, comprising two heavy chains with different amino acid sequences and a binding polypeptide. The heterodimer antibody, or the antigen-binding fragment thereof, include a first heavy chain comprising none or one or more modifications and the second heavy chain comprises one or more modifications and is fused to a binding polypeptide, which can form a isopeptide bond with a binding peptide. The present disclosure further provides systems and methods for purifying such heterodimeric antibodies, and antigen-binding fragments thereof.

Compounds according to formula (I) are described wherein R1 is an amino acid or a modified amino acid linked to the compound through a peptide bond, R2 is selected from CN, SO2CH3, NO2, CO2R3, CONHR3, NH2, NMe2 and CF3, and R3 is selected from H or lower alkyl, X is O or S, and Y is C—H or N, or a pharmaceutically acceptable salt thereof. The compounds can be used as protein disulfide isomerase inhibitors. The compounds can also be used in a method of treating or cancer in a subject.

This invention relates to the field of microbial self-assembled protein fibrils as novel bionanomaterials. More specifically, this invention relates to protein nanofibril materials comprising Bacillus endospore appendage (ENA) proteins, which are spontaneously folded helical hairpin subunits assembled into α-helical multimers (A-ENA) fibrils having a hydrophobic core and covalently linked by one or more isopeptide bonds, providing nanofibrils with high stability and tensile strength. This invention also relates to said protein nanofibrils being engineered or modified to provide functionalized bionanomaterials. In particular, this invention relates to methods for the recombinant preparation of said self-assembled protein nanofibrils, and their use in modifying bacterial endospores and endospore activity or pathogenicity.

This invention provides a nanoparticle protein, MntC-rePO@LS, its preparation method, and its applications. This protein is formed by the covalent binding of MntC@LS and recombinant V antigen-outer membrane protein OprI (rePO) via heteropeptide bonds, creating a dual-nanoparticle vaccine molecule. The recombinant protein SpyCatcher-MntC@LS of this invention can be induced to express in soluble form in *E. coli* and can bind efficiently to the recombinant protein rePO-SpyTag under mild conditions. The nanoparticle protein of this invention can induce a high level of immune response in animals, exerting an immunoprotective effect. Experiments show that its rate of antibody response induction and protective efficiency are significantly superior to those of monomeric MntC, monomeric rePO, and their physical mixtures, and it can be used for the prevention and treatment of *Pseudomonas aeruginosa* and / or *Staphylococcus aureus* infections.

The present invention relates to peptide tags and binding partners which are capable of interacting via the spontaneous formation of an isopeptide bond, as well as to associated peptide pairs and methods for designing peptide tags, binding partners and peptide pairs with improved properties.

This application discloses a method for processing protein samples for mass spectrometry detection. The method involves processing the protein sample into peptides using only ultrasound to obtain a protein sample suitable for mass spectrometry detection, without the use of enzymatic digestion. By precisely controlling the power, time, and mode of ultrasound, the high shear force generated by ultrasonic cavitation directly acts on the peptide bonds of the protein, achieving random and non-specific breakage. This method significantly reduces the protein sample pretreatment time from hours in existing enzymatic methods to minutes, eliminates the need for expensive enzymes, significantly reduces detection costs, simplifies the operation process, and can generate peptides of varying lengths covering the entire protein sequence, providing complementary protein sequence coverage information to enzymatic methods. This offers a novel and efficient solution for protein identification and structural analysis.

A light-initiated chemiluminescence detection method, a reagent, and a use. The detection method comprises: bringing a sample to be tested into contact with a reaction system comprising a first antibody and a second antibody, so as to obtain an immune reaction product, and measuring the optical signal intensity of the immune reaction product, the first antibody and / or the second antibody directionally coupling a non-specific binding region thereof to a target substance by means of an isopeptide bond. Alternatively, an R3 reagent is added on the basis of a conventional detection method, and at least two label molecules are bound by means of a pairing molecule contained in the R3 reagent, the label molecules being carried by the first antibody in luminescent microspheres, such that the at least two luminescent microspheres are aggregated into a multimeric luminescent microsphere. The detection method can improve the detection performance of light-initiated chemiluminescence, and meet detection requirements of a low-abundance sample such as p-tau217 in a blood sample.

The present disclosure provides programmable base editors, and methods for their production and use. A subject programmable base editor includes (1) a CRISPR-Cas fusion protein comprising a CRISPR-Cas effector protein fused to a first member of a split-protein binding pair, where the CRISPR-Cas effector protein is a nickase (e.g., nCas9) or is catalytically inactive (e.g., dCas9, dCas12 such as dCas12a), and (2) a deaminase fusion protein comprising a deaminase protein fused to a second member of the split-protein binding pair. The CRISPR-Cas effector protein and the deaminase protein are not translationally fused to one another, but are instead post-translationally bound, e.g., in some cases covalently linked via a covalent bond (e.g., an isopeptide bond) formed between the two members of the split-protein binding pair (e.g. between a catcher protein and a partner tag protein).

This invention relates to a method for preparing oyster sauce, particularly a method based on the synergistic preparation of oyster sauce using bacterial-enzyme interaction and gradient temperature-variable thermal reaction. The method includes raw material pretreatment, bacterial-enzyme interaction hydrolysis, and gradient temperature-variable thermal reaction. This invention employs a process route combining bacterial-enzyme interaction with complex hydrolysis and a step-by-step gradient temperature-variable thermal reaction. During bacterial fermentation, endonucleases are responsible for efficiently cleaving peptide bonds within proteins, generating a large number of small peptides and amino acids, providing ample precursor substances for the gradient temperature-variable thermal reaction. These precursors are more readily combined with reducing sugars during the reaction. Exonucleases, on the other hand, hydrolyze hydrophobic terminal peptide bonds, reducing the production of bitter peptides and improving the product flavor. The subsequent gradient temperature-variable thermal reaction generates basic aroma substances at low temperatures, followed by a deeper reaction at high temperatures, forming complex and rich aroma compounds with flavors such as roasted meat and nuts. These two processes complement each other, jointly constructing the rich flavor and aroma profile of the oyster sauce.

A method for inhibiting scale deposition in a geothermal system, the method includes treating a water stream of the geothermal system with a scale inhibitor composition, wherein the scale inhibitor composition comprises a compound that includes a peptide bond. The compound that includes the peptide bond may be polypeptide, such as polyaspartic acid. The scale inhibitor composition may include a ligand or dispersant polymer.

This invention develops a nanoprotease based on a bimetallic two-dimensional organic nanoframework and explores its catalytic mechanism. This two-dimensional structure achieves a 3-5 fold increase in hydrolysis efficiency by maximizing the accessibility of active sites and reducing mass transfer resistance, significantly outperforming existing reports. Metal doping and organic ligand properties further enhance Lewis acidity, thereby optimizing peptide bond hydrolysis performance. The organic ligand induces protein unfolding through a hydrophobic interface, exposing protein cleavage sites and accelerating the enzymatic reaction rate. CeCuBDC exhibits excellent stability and superior reusability during protein hydrolysis. Furthermore, this material can hydrolyze various proteins and mixed protein samples, and demonstrates outstanding catalytic activity in selectively cleaving peptide bonds containing hydrophobic residues. As a two-dimensional bimetallic MOF nanoprotease, CeCuBDC shows broad prospects for proteomics applications.

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.

The application discloses a method for preparing potato protein feed by using Lactobacillus plantarum fermentation, and belongs to the technical field of microbial fermentation feed. The method uses potato protein powder with a protein content of greater than or equal to 80% and a proline residue proportion of 4% to 5% as raw material, mixes the potato protein powder with water and a fermentable carbon source, sterilizes the mixture, and inoculates Lactobacillus plantarum and acid protease at the same time to perform anaerobic fermentation. By utilizing the difference between the protease of Lactobacillus plantarum and the acid protease in the optimal pH, the relay hydrolysis of the two proteases in the time dimension is triggered by the natural acid production in the fermentation, and the bottleneck that the proline peptide bond in the potato protein is difficult to be fully hydrolyzed by the conventional bacterial protease is effectively solved. The obtained product has the advantages of significantly improved protein hydrolysis degree and in-vitro digestion rate, greatly increased free proline content, simple process, and the like, and the processing of the potato protein feed is effectively promoted from the increment mode to the quality improvement level, so that the method has a good industrial application prospect.