Patents
Literature
Hiro is an intelligent assistant for R&D personnel, combined with Patent DNA, to facilitate innovative research.
Hiro

571 results about "Peptide bond" patented technology

A peptide bond is an amide type of covalent chemical bond linking two consecutive alpha-amino acids from C1 (carbon number one) of one alpha-amino "acid" and N2 (nitrogen number two) of another along a peptide or protein chain.

Process for producing drug complexes

A method for preparing a drug complex in which a polysaccharide derivative having carboxyl groups and a residue of a drug compound are bound to each other by means of a spacer comprising an amino acid or a spacer comprising peptide-bonded 2 to 8 amino acids, or a drug complex in which a polysaccharide derivative having carboxyl groups and a residue of a drug compound are bound to each other without the spacer, characterized in that an organic amine salt of the polysaccharide derivative having carboxyl groups is reacted with the drug compound or the spacer bound to the drug compound in a non-aqueous system. The reaction between the polysaccharide derivative having carboxyl groups and the drug compound bound with the spacer or the like can be carried out in high yields, and when a drug compound having a lactone ring is subjected to the reaction, side reactions can be reduced.
Owner:DAIICHI PHARMA CO LTD

Peptide capable of binding to nanographite structures

It is intended to provide a peptide or a phage recognizing nanographite structures and thus enabling efficient recognition, binding, separation and alignment of nanographite structures such as carbon nanohoms or carbon nanotubes, an artificial protein or a chimeric molecule comprising the above-described peptide bonded to a functional peptide, a protein, a labeling, etc., and a complex of the above-described peptide molecule, artificial protein or chimeric molecule with a nanographite structure. By panning peptide-presenting phages bonded to nanographite structures, a nanographite structure-binding peptide capable of specifically recognizing nanographite structures such as carbon nanohoms or carbon nanotubes is obtained.
Owner:JAPANESE FOUND FOR CANCER RES +1

Heterodimeric fusion proteins useful for targeted immune therapy and general immune stimulation

InactiveUS20050137384A1Extended half-lifeAltering pharmacology and biodistributionPeptide/protein ingredientsAntibody mimetics/scaffoldsWhite blood cellStepwise approach
Disclosed are methods for producing fusion proteins with the heterodimeric cytokine, interleukin-12. In order to insure that the proper ratio of fused and non-fused subunits are obtained in the fusion protein, a specific stepwise approach to genetic engineering is used. This consists of first expressing the non-fused p40 IL-12 subunit in a production cell line, followed by or simultaneously expressing in the same cell, a second recombinant fusion protein consisting of the fused polypeptide linked by a peptide bond to the p35 subunit of IL-12. Molecules containing the p35 fusion protein cannot be secreted from the transfected mammalian cell without first complexing in a one to one ratio with the p40 subunit, thus ensuring the production of active heterodimeric fusion proteins.
Owner:MERCK PATENT GMBH

Thiosuccinic Acid Derivatives and the Use Thereof

The present invention relates to compounds of the Formula (I), wherein X1 and X2 independently represent O, NH or S; R1 and R2 are independently selected from the group consisting of a C1-C30 hydrocarbyl group, an amino acid bonded via an amide bond or a peptide bonded via an amide bond each having up to 200 amino acids, the conjugated residue X1 or X2 in this case being NH, and hydrogen, both radicals R1 and R2 preferably not being H; and R3 is a residue selected from group consisting of —S—R6, wherein R6 is a C1-C30 hydrocarbyl group, at least one of R1 and R2 not being H when X1 and X2 are oxygen, —S—CH2—CH(NH2)(COOH) (cysteine-S-yl), a homologue or derivative (e.g. N-acetyl cysteine-S-yl) thereof, a peptide having up to 200 amino acids which contains at least one amino acid radical with a thiol group, preferably a cysteine radical, and is bonded via the thio sulfur, preferably via the cysteine sulfur (peptide-S-yl), coenzyme A which is bonded via a thiol group or fragments thereof, acyl carrier protein bonded via a thiol group, and dihydrolipoic acid bonded via a thiol group; and pharmaceutically acceptable salts thereof. The present invention also relates to the use of these compounds for preparing a drug, drugs containing the same and their use for the therapy of diseases such as autoimmune disease, NF-kappaB mediated diseases, psoriasis, psoriatic arthritis, neurodermitis, enteris regionalis Crohn, cardiac insufficiency, chronic obstructive pulmonary diseases and asthma and in transplantation medicine.
Owner:BIOGEN INT

Chaperonin-target protein complex, method of producing the same, method of stabilizing target protein, method of immobilizing target protein, method of analyzing the structure of target protein, sustained-release formulation, and method of producing antibody against target protein

InactiveUS20070059794A1Excessive immune responseEfficient executionSugar derivativesHydrolasesProtein targetChaperonin
The present invention provides a chaperonin-target protein complex and a method of producing the same, and a method of stabilizing the target protein, a method of immobilizing the target protein, a method of analyzing the structure of the target protein, a sustained-release formulation, and a method of producing an antibody against the target protein. The chaperonin-target protein complex in the present invention includes a fusion protein having a chaperonin subunit and an affinity tag linked to the chaperonin subunit via a peptide bond and a target protein for which the affinity tag shows a specific affinity, wherein the target protein is bound to the affinity tag by means of the specific affinity, thereby forming a chaperonin ring structure consisting of a plurality of chaperonin subunits. The chaperonin-target protein in the present invention stabilizes the target protein and surely immobilize on a carrier without causing any change in its stereostructure.
Owner:SEKISUI CHEM CO LTD

Preparation method of fermented rice sticks

ActiveCN101623065APlay the effect of debranching and straighteningShorten fermentation timeFood preparationAmylaseProteinase activity
The invention relates to a preparation method of fermented rice sticks, which belongs to the field of food fermentation and comprises a pulp making procedure and a pulp steaming procedure. The preparation method of fermented rice sticks is characterized in that 1-1000ml of debranching amylase for per 100kg of rice is added into rice pulp with the weight percent of 5 to 50% before the pulp steaming procedure and after the pulp making procedure, the pH value is regulated to 4.0-5.0, and enzymolysis is carried out for 30-360 min under the temperature of 30-60 DEG C; 1-50 g of protease with proteolysis peptide bonds for per 100kg of rice is added into the rice pulp, and enzymolysis is carried out for 60-360 min under the temperature of 30-60DEG C and the pH value of 4.0-8.0; then, 0.2 ml/kg of zymophyte is added to the pulp and fermented for 360-3600 min under the temperature of 25-30DEG C and the pH value of 5.0-6.0. In the invention, the debranching amylase is utilized to hydrolyze Alpha-D-1, 6 glycoside bonds as the branched chains in starch and dextrine to generate straight-chain compound sugar containing Alpha-D-1, 4 glycoside bonds so as to obtain the effect on debranching and adding straight chains; the protease with proteolysis peptide bonds can be used for hydrolyzing molecular protein and amino acid to provide sufficient amino acid for following mixed fermentation, shorten fermentation time, and improve the quality and the taste of products.
Owner:江西蓓蕾食品有限公司

Amphipathy triblock polymer and preparation method and application thereof

The invention relates to an amphipathy triblock polymer. The amphipathy triblock polymer is a linear compound comprising a hydrophilic chain section, an intermediate chain section and a hydrophobic chain section, wherein the hydrophilic chain section is a polyethylene glycol derivative; the intermediate chain section is a peptide polymer comprising lysine, leucine and glutamic acid; the hydrophobic chain section is polyphenylalanine; the polyethylene glycol derivative is connected with one end of the intermediate chain section through an amido bond; and the polyphenylalanine is connected with the other end of the intermediate chain section through a peptide bond. The amphipathy triblock polymer provided by the invention can be self-assembled in an aqueous solution to form a polymer nano-micelle with a three-layer structure; the polymer nano-micelle servicing as a vector has the characteristics of high stability, excellent biocompatibility and the like; the amphipathy triblock polymer is hardly removed by the immune system during circulating in a human body, and hydrophobic small molecule drugs, genetic materials and protein molecules can be effectively loaded at the same time, so that the amphipathy triblock polymer has a wide application prospect. In addition, the invention also provides a preparation method of the amphipathy triblock polymer.
Owner:SHENZHEN INST OF ADVANCED TECH

Method For The Manufacture Of Degarelix

In a step-wise synthesis of degarelix comprising 0.3 % by weight or less of 4-([2-(5-hydantoyl)]acetylamino)-phenylalanine analog on (solid support)-NH2 a step comprises providing a solution of an amino acid or peptide of which the a-amino group is protected by Fmoc; contacting the support with the solution in the presence of reagent for forming a peptide bond between a carboxyl group of the amino acid or peptide and (solid support)-NH2; removing Fmoc by contacting the support with an organic base, in particular piperidine, in an organic solvent. Also disclosed is degarelix of high purity prepared by the method of the invention and the use of Fmoc in the synthesis of degarelix.
Owner:POLYPEPTIDE LAB AS
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products