199 results about "Peptide bond" patented technology

This invention provides a tetrahedral antibody comprising a first, second, third, and fourth domain, wherein the first and second domains are Fab or Fc domains; wherein each of the first and second domains comprise a first polypeptide chain comprising a first N-terminus of the domain, and a second polypeptide chain comprising a second N-terminus of the domain; wherein the first N-terminus of the first domain and the first N-terminus of the second domain are joined to each other by a non-peptidyl linkage, which can be a covalent linkage or a non-covalent linkage between first and second dimerizing polypeptides attached to the first N-termini of the first and second domains, respectively; and wherein the third and fourth domains are attached at their respective C-termini to the second N-termini of the first and second domains, respectively, or the N-termini of the first and second dimerizing polypeptides.

The invention discloses methanogen lyase homologous with a PeiR lyase sequence and application of the methanogen lyase, and aims to solve the problem that PeiR lyase protein of a methanogen cell wall peptide bond can participate in a biological process of hydrolyzing archaea cell walls, effectively kill methanogen and reduce methane production, and protein homologous with the PeiR lyase protein has potential methane reduction potential. According to the invention, a series of biological information software is utilized to identify protein sequences coded by methanogens virus from rumen microbiome sequencing data, and sequence homology between the proteins and PeiR protein is further analyzed to obtain a series of methanogens lyases. In order to realize the expression of the lyase, multiple segments of primers are designed to synthesize a target sequence, and the target sequence is successfully expressed in a prokaryotic expression system. Through the detection of crude enzyme liquid, the effectiveness of the lyase in the aspect of reducing the methane yield is verified in an in-vitro gas production test.

The invention discloses methanogen lyase homologous with high-dimensional characteristics of PeiW lyase and application of the methanogen lyase, and aims to solve the problem that PeiW lyase protein of methanogen cell wall peptide bonds can participate in the biological process of hydrolyzing archaea cell walls, effectively kill methanogen and reduce methane production, and protein homologous with the protein has potential methane reduction potential. According to the method, a series of bioinformatics software is utilized, a protein sequence coded by methanogens virus is identified from a large amount of rumen microorganism virus group sequencing data, the high-dimensional homology of a deep learning model between the protein sequence and PeiW is analyzed, and two methanogens lyases similar to the high-dimensional characteristics obtained by the PeiW model are obtained. In order to realize the expression of the lyase, multiple segments of primers are designed to synthesize a target sequence, and the target sequence is successfully expressed in a prokaryotic expression system. Through detection of a crude enzyme solution, the effectiveness of the lyase in the aspect of reducing the yield of methane is verified in an in-vitro gas production test.

The invention discloses methanogen lyase with the same protein family annotation as PeiR lyase and application of the methanogen lyase, and the methanogen lyase is obtained through homologous screening of Pfam protein family database annotation based on known PeiR lyase characteristics aiming at methanogen cell wall peptide bonds. The PeiR lyase protein can participate in the biological process of hydrolyzing archaea cell walls, methanogens are effectively killed, methane production is reduced, and the protein homologous with the protein has potential methane reduction potential. According to the invention, by integrating metagenome sequencing data of rumen microorganisms, screening methanogenic bacterium virus protein by using series bioinformatics software, and combining Pfam functional domain annotation to carry out homologous relationship analysis, a series of lyase is finally identified and is successfully expressed in a prokaryotic expression system, and meanwhile, an in-vitro gas production experiment result also shows that the methanogenic bacterium virus protein can be successfully expressed in a prokaryotic expression system. The crude enzyme liquid can significantly reduce the methane generation amount.

The invention discloses methanogen lyase homologous with high-dimensional characteristics of PeiR lyase and application of the methanogen lyase and aims to solve the problems that PeiR lyase protein of methanogen cell wall peptide bonds can participate in the biological process of hydrolyzing archaea cell walls, methanogen is effectively killed, methane production is reduced, and protein homologous with the protein has potential methane reduction potential. According to the invention, a series of biological information software is utilized to identify protein sequences coded by methanogen viruses from a large amount of rumen microbiome sequencing data, and high-dimensional homology between the proteins and PeiR proteins based on a deep learning model TM-Vec is further analyzed, so that a series of methanogen lyases are obtained. In order to realize the expression of the lyase, multiple segments of primers are designed to synthesize a target sequence, and the target sequence is successfully expressed in a prokaryotic expression system. Through the detection of crude enzyme liquid, the effectiveness of the lyase in the aspect of reducing the methane yield is verified in an in-vitro gas production test.

The present invention relates to a polymer having a main chain, wherein the main chain comprises linear amide bonds and a heteromonocyclic moiety containing a nitrogen atom, wherein the main chain does not contain peptide bonds, or wherein, based on the total number of linear amide bonds in the main chain, the proportion of peptide bonds in the main chain is at most 30%, and wherein, based on the total weight of the polymer, the proportion of the heteromonocyclic moiety containing a nitrogen atom is from 5% by weight to 25% by weight. The present invention also relates to a product or article and the use of the polymer for manufacturing or producing the product or article.

The present invention relates to a compound binding to an endogenous receptor, said compound comprising (i) an oligopeptide comprising a dipeptide with Trp being the C-terminal amino acid of said dipeptide, wherein said Trp is replaced with an α-amino acid Xaa2, whereby the stability in serum or plasma of the peptide bond connecting Xaa2 to the N-terminally adjacent amino acid is increased as compared to the peptide bond connecting Trp to the N-terminally adjacent amino acid in an otherwise identical compound; and (ii) a moiety capable of generating therapeutically effective radiation, said moiety being covalently bound to said oligopeptide.

The invention provides an amino acid skeleton ionizable lipid as well as a preparation method and application thereof, the amino acid skeleton ionizable lipid is modified by taking amino acid as a core, has more ester groups and peptide bonds, and can be quickly hydrolyzed by enzyme after RNA is effectively released in vivo; the transfection body is provided with four tail structures, the cross sectional area of the lipid tail can be increased, drugs such as RNA are helped to escape from an endosome, and then the transfection effect is enhanced; the charge capable of ionizing the lipid is electrically neutral under physiological conditions, so that the cytotoxicity caused by excessive positive charges is reduced, the stability of the lipid nanoparticles is further improved, the cycle time of the loaded nucleic acid medicine is prolonged, and the pharmacokinetic characteristics are improved. The LNP prepared from the ionizable lipid, auxiliary phospholipid, cholesterol and PEG lipid provided by the invention has more excellent nucleic acid carrier performance, and can effectively deliver nucleic acid drugs such as siRNA, mRNA, pDNA and the like into cells to play a role.

There is provided peptidic compounds of Formula I, A or B(Rradn6-[linker]-RL-Xaa1-Xaa2-Xaa3-Xaa4-Xaa5-Xaa6-Xaa7-Xaa8-ψ-Xaa9-NH2). Xaa1 is D-Phe, Cpa, D-Cpa, Nal, D-Nal, 2-Nal, or D-2-Nal; Xaa2 is Asn, Gln, Hse, Cit or His. Xaa3 is Trp, Bta, Trp(Me), Trp(7-Me), Trp(6-Me), Trp(5-Me), Trp(4-Me), Trp(2-Me), Trp(7-F), Trp(6-F), Trp(5-F), Trp(4-F), Trp(5-OH), or αMe-Trp. Xaa4 is Ala or Ser. Xaa5 is Val, Cpg, or Tle. Xaa6 is Gly, NMe-Gly, or D-Ala. Xaa7 is His or NMe-His. Xaa8 is Leu or Phe. Xaa9-NH2 is a C-terminally amidated amino acid residue selected from Pro, 4-oxa-L-Pro, Me2Thz, or Thz. ψ represents a peptide bond or reduced peptide bond joining Xaa8 to Xaa9. Rradn6 is 1-5 radiolabeling groups. There is also provided the use of such compounds as imaging agents or therapeutic agents.

A compound comprising a prostate specific membrane antigen (PSMA)-targeting moiety of the following formula (I) or of a salt or a solvate thereof. R1 is —R1aR1b— wherein R1a is absent, —CH2—, —O—, or —S—, and R1b is —CH2— or —CHF—. R2 is —(CH2)3—O—, —(CH2)3—, —(CH2)4—, —CH2—O—(CH2)2—, or —CH2—S—(CH2)2. R3 is ethylene fused to a tricyclic fused ring. L1, L2, L3, L4, L5b L5c, L6 and L7 are linkages (e.g. peptide bonds). Xbr is a branching atom. Rrad is a radiometal chelator. Ralb is an albumin binder. n1, n2, n3, n4, and n5 are integers. When the PSMA-targeting moiety is linked to a radiolabeling group, the compound may be used as an imaging agent or therapeutic agent for PSMA-expressing diseases / conditions.

Compositions and related methods and uses are provided comprising sotebercept and variants thereof wherein the variants undergo a peptide bond cleavage between arginine 4 and serine 5 (Arg (4)-Ser (5) of the amino acid sequence (SEQ ID NO: 2) of one or two monomeric peptide chains of sotebercept, calculated based on peptide mass fingerprinting analysis, and wherein the variants have a peptide bond cleavage between arginine 4 and serine 5 (Arg (4)-Ser (5) of one or two monomeric peptide chains of sotebercept. The variant content is less than or equal to about 10%. The invention further provides a pharmaceutical preparation containing the composition and a preparation method of the pharmaceutical preparation. In addition, the invention also provides a detection method of the variant and application of the variant in quality inspection or quality control of a product containing sotebercept.

The invention relates to molecular glue for forming fimbriae related protein based on SpaA isopeptide bonds of Vinci bacteria. The invention also relates to a nanoparticle vaccine composition formed by the molecular glue, and the immunogen is covalently displayed on the surface of the nanoparticle by the molecular glue.

The invention belongs to the technical field of enzyme engineering and gene engineering, and particularly relates to a recombinant immobilized enzyme, an expression gene thereof and application of the recombinant immobilized enzyme in production of macrocyclodextrin. According to the preparation method, SpyTag and SpyCatcher peptides are fused to the N end of isoamylase and the N end of 4-alpha-glucanotransferase respectively, the 4-alpha-glucanotransferase modified by the SpyTag and the isoamylase modified by the SpyCatcher are obtained, and after spontaneous isopeptide bonds are formed between the SpyTag and the SpyCatcher, the self-assembled macrocyclodextrin production enzyme cluster is obtained. The obtained macrocyclodextrin production enzyme cluster forms an enzyme aggregate with a three-dimensional structure under the traditional glutaraldehyde-mediated catalytic action, namely the recombinant immobilized enzyme. The recombinant immobilized enzyme disclosed by the invention can be repeatedly utilized, is simple and convenient to operate, is easy to separate a converted product, and can be applied to industrial production of the macrocyclodextrin.

The present invention pertains to specific bioparticules at the surface of which are expressed multimeric protein. The bioparticles according to the present invention comprise an envelope consisting of a plasma membrane; and at least one type I or II transmembrane fusion protein anchored in said membrane, said fusion protein comprising successively a) a first monomer of a multimeric protein of interest, b) a coiled-coil domain or oligomerization sequence; and c) a domain for anchoring in the plasma membrane, consisting of a transmembrane segment and a cytosolic segment. Fragments a) and b) are exposed at the surface of the bioparticle, and fragment a) is bound to a second monomer of said multimeric protein by means of a bond which is not a peptide bond. The bioparticles according to the present invention can be used in therapy such as immunotherapy. The present invention also pertains to methods for producing such bioparticles.

The invention discloses a sea-buckthorn small molecule peptide and a preparation method thereof, and relates to the field of biological medicine and food processing. According to the method, sea-buckthorn pulp residues and sea-buckthorn seed residues are used as composite raw materials and are mixed and stirred to form homogenate, and then cell wall structures are destroyed through ultrasonic wall breaking treatment to release protein components; then cutting off a peptide bond under the action of compound enzymes (plant protease, neutral protease and pepsase) by adopting an ultrasonic-enzyme synergistic hydrolysis process to generate a small molecule peptide fragment; after removing impurities through centrifugal separation, purifying through an ultrafiltration membrane (the molecular weight cut-off is 1-3kDa) to obtain a small molecule peptide solution; and performing debitterizing treatment by using macroporous adsorption resin, and preparing sea-buckthorn small molecule peptide powder by using a vacuum freeze-drying technology. According to the method, through ultrasonic-enzyme synergistic interaction, multi-stage purification combination and low-temperature keep-alive processes, the yield, molecular weight uniformity and antioxidant activity of small molecular peptides are remarkably improved, and high-valued utilization of sea-buckthorn processing by-products is achieved.

The invention discloses an in-vitro biochemical test method for evaluating the anti-wrinkle effect of cosmetics and raw materials. The in-vitro biochemical test method comprises the following steps: step 1, preparing a working solution; 2, preparing a sample solution; step 3, adding an enzyme working solution; step 4, loading samples in groups; 5, adding a substrate and reacting; step 6, developing treatment; step 7, determining absorbance; 8, calculating, analyzing and processing data; and step 9, result judgment: analyzing and evaluating the anti-wrinkle effect of the sample through a statistical means. According to the method, based on a collagenase inhibition test, when peptide bonds between GLY and GLY in Z-GLY-PRO-GLY-GLY-PRO-ALA-OH are specifically hydrolyzed by collagenase, GLY-PRO-ALA is released, and the activity of the collagenase is indirectly evaluated by measuring the change of a light absorption value at 565 nm after the GLY-PRO-ALA reacts with a color developing agent, so that whether a sample to be detected has an anti-wrinkle effect or not is judged. The method is economical and fast, the test process is controllable, the test system is standardized, and result deviation caused by individual difference can be avoided.

The invention relates to a surface display system based on an isopeptide bond and a construction method and application of the surface display system, two conformational proteins including an anchor protein containing the isopeptide bond and a target protein are designed through a modularization method, and through covalent coupling formed between lysine and asparagine or aspartic acid residues in a molecular adhesive system based on the isopeptide bond, the surface display system based on the isopeptide bond is obtained. And displaying the target protein on the surface of escherichia coli. According to the surface display system based on the isopeptide bond, high-efficiency display of complex enzyme and macromolecular protein on the cell surface is realized, and the influence of direct fusion with anchoring protein on the activity of target protein is avoided. According to the constructed surface display whole-cell catalyst, the tedious enzyme purification process is omitted, the stability of the enzyme is improved, the production cost is lower, and the surface display whole-cell catalyst shows a good application prospect in biological catalysis.

This invention discloses methanogenic lyases with the same protein family annotation as PeiR lyases and their applications. These enzymes are obtained through homology screening based on the known characteristics of PeiR lyases targeting peptide bonds in the methanogenic cell wall, using the Pfam protein family database annotation. PeiR lyase proteins participate in the biological process of hydrolyzing archaea cell walls, effectively killing methanogens and reducing methane production. Proteins homologous to this protein have potential methane-reducing potential. This invention integrates rumen microbial metagenomic sequencing data, uses a series of bioinformatics software to screen methanogenic viral proteins, and combines Pfam functional domain annotation for homology analysis, ultimately identifying a series of lyases. These lyases were successfully expressed in a prokaryotic expression system, and in vitro gas production experiments also showed that the crude enzyme solution significantly reduced methane production.

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.

The invention relates to the technical field of enzyme engineering and food processing, and particularly discloses a method for preparing soybean meal peptide through solid enzymolysis of soybean meal with a compound enzyme. According to the method, alkaline protease, neutral protease and trypsin are compounded into a compound enzyme according to the mass ratio of 1: 1: 1, and the yield and quality of the soybean meal peptide are remarkably improved by optimizing solid enzymolysis process conditions, the temperature is 50 DEG C, the pH is 6.5, the time is 7 hours and the material-liquid ratio is 1: 0.5. The hydrolysis degree reaches 24.61%, the peptide yield reaches 14.77%, the material-liquid ratio is reduced to 1: 0.5 compared with a traditional liquid method, near-zero wastewater discharge is achieved, and the environmental protection cost is reduced. Fourier infrared spectroscopy verifies that the peptide bond structure of the product is complete (the amide I band is 1650 cm <-1 >), and the secondary conformation is mainly beta-folding. The invention provides a low-cost, low-energy-consumption and sustainable soybean meal peptide industrial production scheme for environment-friendly strictly-controlled areas and small and medium-sized enterprises, and has the advantages of high resource value and green process.

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.

The invention discloses a fatty cation amphiphilic peptide simulant as well as a preparation method and application thereof. The preparation method comprises the following steps: firstly, developing an amphipathic cationic peptide simulant system based on cysteine, then introducing ethylenediamine as a cationic group by forming a peptide bond at the terminal of carboxyl, and introducing a hydrophobic group containing an aromatic ring to a sulfydryl side chain; wherein the cationic group provides positive charges and hydrophilicity and is beneficial to electrostatic interaction with a bacterial membrane with negative charges, and the hydrophobic group is beneficial to insertion of the membrane into a phospholipid bilayer; in addition, the N terminal is modified by fatty acids with different chain lengths, the amphiphilic balance of the cysteine-based cationic peptide simulant is finely adjusted, and finally the fatty cationic amphiphilic peptide simulant is synthesized. The peptidomimetic has good antibacterial activity, is not easy to induce bacteria to generate drug resistance, and can be used for preparing drugs for treating, improving and / or preventing infection of drug-resistant bacteria and / or drug-resistant fungi.

This invention provides, inter alia, for an aza GLP-l-based therapeutic analogue wherein at least one peptide bond of a GLP-1-based therapeutic peptide has been replaced with an azapeptide or azatide bond.

The present invention relates to vaccine compositions, most notably vaccine compositions wherein the antigenic component is large, for example over 50 kDa, or multimeric, i.e. comprised of subunits. Such antigenic components are of particular interest, because they may represent antigenic components from pathogens that currently it is not possible to vaccinate against. The invention relates to a composition comprising a particle displaying an antigenic component, wherein said composition comprises an antigenic component comprising a first peptide tag, and a moiety comprising a second peptide tag, wherein the antigenic component and the moiety are linked via an isopeptide bond between said first and second peptide tags, and wherein the antigenic component is over 50 kDa, or alternatively is multimeric.

The present invention relates to a method for modifying meat, including bringing the meat in contact with a Bacillus amyloliquefaciens-derived neutral protease having the following properties (a) to (e), and thermolysin; (a) being an enzyme that hydrolyzes a substrate having a peptide bond to release the peptide, (b) having an optimal pH of 7, (c) being stable at pH=5 to 7, (d) having an optimal temperature of 50°C to 55°C, (e) being a metal protease inhibited by ethylenediaminetetraacetic acid (EDTA), and a composition for modification, containing said neutral protease and thermolysin. According to the present invention, meat can be tenderized conveniently in a short time, and ease of loosening can be imparted to the meat.

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 invention discloses a synthesis method of ubiquitin (1-74) NHNH2, and belongs to the technical field of protein synthesis. The synthesis method comprises the following steps: utilizing a prokaryotic expression system, expressing a full-length protein of Ub (1-76) and a Josephin protein coded by Burkholderia pyrrocinia by virtue of an escherichia coli BL21 (DE3) strain, hydrolyzing the Ub (1-76) by virtue of the obtained 6His-BpJOS, cutting a peptide bond between Ub Arg-74 and Gly-75, and capturing a generated thiolipid intermediate by virtue of hydrazine hydrate, so as to obtain the Ub (1-74) NHNH2. According to the present invention, the ubiquitin cleavage enzyme BpJOS catalyzed in-situ activation process is adopted, such that the preparation yield is high, the operation is simple, the large-scale preparation can be achieved, the synthesis cost is low, and the method can be used for synthesizing the multi-ubiquitination modified fragment and synthesizing the Ub (1-74) probe as the precursor, and has wide application prospects.

The present invention relates to a polypeptide forming one part of a two-part linker wherein the polypeptide (protein) spontaneously forms an isopeptide bond with a peptide tag, i.e. The other part of the two-part linker. The invention also relates to a method for producing a polypeptide of the invention and to the use of said polypeptide. According to the present invention, the reaction rate of the Sdy-Catcher variant obtained through mutation is significantly improved compared to the reaction rate of Sdy-Tag, such that the ideal direction is provided for the searching of polypeptides with characteristics of high binding rate and good binding effect in the field.

The invention discloses a preparation method and application of a high-strength, mildew-proof and low-cost cottonseed meal protein adhesive. The preparation method comprises the following steps: compounding L-lysine and 4-carboxyphenylboronic acid through a coupling reaction to prepare lysine borate, adding the prepared lysine borate into the cottonseed meal protein adhesive, adding a proper amount of transglutaminase, and uniformly stirring to obtain the novel high-strength, mildew-proof and low-cost cottonseed meal protein adhesive based on the skin bionic strategy. The innovation points of the invention are as follows: by simulating a peptide bond between protein and polysaccharide in skin and forming a compact cross-linked layer through dehydration condensation reaction, using transglutaminase to construct a grain-lysine isopeptide bond, and introducing boric acid to form a covalent boron-oxygen-six-ring structure, a dual cross-linked network is constructed. The cottonseed meal protein adhesive has the advantages that the bonding strength, mildew resistance and other properties of the cottonseed meal protein adhesive can be remarkably improved only by using trace transglutaminase and boron oxygen six-ring as cross-linking agents, and the preparation cost of the adhesive is reduced.

The invention relates to a molecular peptide mutant, the amino acid sequence of which is as shown in SEQ ID NO: 1. In the invention, SpyCatcher is designed and modified to obtain a molecular peptide SpyCatcher-21 with stimulus response to pH on the basis of not affecting the formation of isopeptide bonds, and Pro is introduced into a key loop of the SpyCatcher-21 through analysis of the crystal structure to reduce the flexibility of the loop and obtain a mutant SpyCatcher-21_A82P, which can raise ligation efficiency with SpyTag. The SpyCatcher-21_A82P can be used to achieve double-enzyme catalysis according to objective needs by changing the pH of the environment to obtain different degrees of coupling, or obtain a three-enzyme coupled catalytic system through electrostatic interaction with a positively charged enzyme.