NATIONAL UNIVERSITY CORPORATION KAGOSHIMA UNIVERSITY (Japon)
NATIONAL UNIVERSITY CORPORATION CHIBA UNIVERSITY (Japon)
Inventeur(s)
Komoto, Shota
Ogawa, Yu
Shoyama, Yoshinari
Hatano, Tadashi
Ito, Yuji
Arano, Yasushi
Suzuki, Hiroyuki
Uehara, Tomoya
Abrégé
Described is a labeling technique which can facilitate the metabolism in the liver after administration to patients without the reduction in the antibody function, thereby reducing accumulation of radionuclides in an organ such as the liver, and a modified antibody containing an IgG antibody and an IgG-binding peptide bound to the IgG antibody. The IgG-binding peptide has an amino acid sequence consisting of 13 to 17 amino acid residues, such as GPDCAYH(Xaa1)GELVWCTFH (SEQ ID NO: 2) wherein Xaa1 represents a lysine residue, a cysteine residue, an aspartic acid residue, a glutamic acid residue, 2-aminosuberic acid, or diaminopropionic acid, and a compound represented by the following formula (II-1) is linked at a position of the lysine residue via a modification linker to the N terminus of the IgG-binding peptide.
A61K 47/68 - Préparations médicinales caractérisées par les ingrédients non actifs utilisés, p. ex. les supports ou les additifs inertesAgents de ciblage ou de modification chimiquement liés à l’ingrédient actif l’ingrédient non actif étant chimiquement lié à l’ingrédient actif, p. ex. conjugués polymère-médicament l’ingrédient non actif étant un agent de modification l’agent de modification étant un anticorps, une immunoglobuline ou son fragment, p. ex. un fragment Fc
A61K 51/10 - Anticorps ou immunoglobulinesLeurs fragments
C07K 5/065 - Dipeptides la chaîne latérale du premier amino-acide contenant des carbocycles, p. ex. Phe, Tyr
C07K 5/087 - Tripeptides la chaîne latérale du premier amino-acide contenant des carbocycles, p. ex. Phe, Tyr
C07D 257/02 - Composés hétérocycliques contenant des cycles comportant quatre atomes d'azote comme uniques hétéro-atomes du cycle non condensés avec d'autres cycles
C07K 7/08 - Peptides linéaires ne contenant que des liaisons peptidiques normales ayant de 12 à 20 amino-acides
C07K 16/32 - Immunoglobulines, p. ex. anticorps monoclonaux ou polyclonaux contre du matériel provenant d'animaux ou d'humains contre des produits de traduction des oncogènes
2.
PHOSPHOLIPID, AND FEED CONTAINING SAME FOR FISH AND SHELLFISH
NATIONAL UNIVERSITY CORPORATION KAGOSHIMA UNIVERSITY (Japon)
Inventeur(s)
Tanaka, Tatsushi
Yokoyama, Saichiro
Abrégé
Provided is a phospholipid to which DHA and/or EPA is bound, wherein: the DHA and/or the EPA is contained at a total amount of 2-50 wt% relative to the entirety of constituent fatty acids in the phospholipid; and (the total amount of DHA and/or EPA bound to position 2 of the phospholipid)/(the total amount of DHA and EPA bound to position 1 and position 2 of the phospholipid)(weight ratio) is 0.2-0.8.
A23K 10/30 - Produits alimentaires pour animaux à base de matières d’origine végétale, p. ex. de racines, de graines ou de foinProduits alimentaires pour animaux à base de matières d’origine fongique, p. ex. de champignons
A23K 20/158 - Acides grasGraissesProduits contenant des huiles ou des graisses
A23K 50/80 - Produits alimentaires spécialement conçus pour des animaux spécifiques pour les animaux aquatiques, p. ex. pour les poissons, les crustacés ou les mollusques
3.
HOLE PROCESSING TOOL, AND DESIGN METHOD, MANUFACTURING METHOD, AND EVALUATION METHOD FOR SAME
NATIONAL UNIVERSITY CORPORATION KAGOSHIMA UNIVERSITY (Japon)
NATIONAL UNIVERSITY CORPORATION CHIBA UNIVERSITY (Japon)
Inventeur(s)
Komoto, Shota
Ogawa, Yu
Shoyama, Yoshinari
Hatano, Tadashi
Ito, Yuji
Arano, Yasushi
Suzuki, Hiroyuki
Uehara, Tomoya
Abrégé
The present invention relates to a labeling technique with which, without deterioration in the function of an antibody, metabolization in the liver after administration to a patient is facilitated and accumulation of radionuclides in organs such as liver is reduced. The present invention provides a modified antibody containing an IgG antibody and an IgG-binding peptide bound thereto. The IgG-binding peptide contains an amino acid sequence comprising 13-17 amino acid residues such as GPDCAYH(Xaa1)GELVWCTFH (wherein Xaa1 is a lysine residue, cysteine residue, aspartic acid residue, glutamic acid residue, 2-aminosuberic acid, or diaminopropionic acid). A compound represented by formula (II-1) is connected at the lysine residue to the N terminal of the IgG-binding peptide through a modification linker.
C07K 16/00 - Immunoglobulines, p. ex. anticorps monoclonaux ou polyclonaux
A61K 47/68 - Préparations médicinales caractérisées par les ingrédients non actifs utilisés, p. ex. les supports ou les additifs inertesAgents de ciblage ou de modification chimiquement liés à l’ingrédient actif l’ingrédient non actif étant chimiquement lié à l’ingrédient actif, p. ex. conjugués polymère-médicament l’ingrédient non actif étant un agent de modification l’agent de modification étant un anticorps, une immunoglobuline ou son fragment, p. ex. un fragment Fc
A61K 47/69 - Préparations médicinales caractérisées par les ingrédients non actifs utilisés, p. ex. les supports ou les additifs inertesAgents de ciblage ou de modification chimiquement liés à l’ingrédient actif l’ingrédient non actif étant chimiquement lié à l’ingrédient actif, p. ex. conjugués polymère-médicament le conjugué étant caractérisé par sa forme physique ou sa forme galénique, p. ex. émulsion, particule, complexe d’inclusion, stent ou kit
A61K 39/395 - AnticorpsImmunoglobulinesImmunsérum, p. ex. sérum antilymphocitaire
A61K 51/10 - Anticorps ou immunoglobulinesLeurs fragments
C07D 257/02 - Composés hétérocycliques contenant des cycles comportant quatre atomes d'azote comme uniques hétéro-atomes du cycle non condensés avec d'autres cycles
C07K 7/06 - Peptides linéaires ne contenant que des liaisons peptidiques normales ayant de 5 à 11 amino-acides
C07K 7/08 - Peptides linéaires ne contenant que des liaisons peptidiques normales ayant de 12 à 20 amino-acides
NATIONAL UNIVERSITY CORPORATION KAGOSHIMA UNIVERSITY (Japon)
NATIONAL UNIVERSITY CORPORATION CHIBA UNIVERSITY (Japon)
Inventeur(s)
Komoto Shota
Ogawa Yu
Shoyama Yoshinari
Hatano Tadashi
Ito Yuji
Arano Yasushi
Suzuki Hiromoto
Uehara Tomoya
Abrégé
The present invention relates to a labeling technique with which, without deterioration in the function of an antibody, metabolization in the liver after administration to a patient is facilitated and accumulation of radionuclides in organs such as liver is reduced. The present invention provides a modified antibody containing an IgG antibody and an IgG-binding peptide bound thereto. The IgG-binding peptide contains an amino acid sequence comprising 13-17 amino acid residues such as GPDCAYH(Xaa1)GELVWCTFH (wherein Xaa1 is a lysine residue, cysteine residue, aspartic acid residue, glutamic acid residue, 2-aminosuberic acid, or diaminopropionic acid). A compound represented by formula (II-1) is connected at the lysine residue to the N terminal of the IgG-binding peptide through a modification linker.
C07K 16/00 - Immunoglobulines, p. ex. anticorps monoclonaux ou polyclonaux
A61K 39/395 - AnticorpsImmunoglobulinesImmunsérum, p. ex. sérum antilymphocitaire
A61K 47/68 - Préparations médicinales caractérisées par les ingrédients non actifs utilisés, p. ex. les supports ou les additifs inertesAgents de ciblage ou de modification chimiquement liés à l’ingrédient actif l’ingrédient non actif étant chimiquement lié à l’ingrédient actif, p. ex. conjugués polymère-médicament l’ingrédient non actif étant un agent de modification l’agent de modification étant un anticorps, une immunoglobuline ou son fragment, p. ex. un fragment Fc
A61K 47/69 - Préparations médicinales caractérisées par les ingrédients non actifs utilisés, p. ex. les supports ou les additifs inertesAgents de ciblage ou de modification chimiquement liés à l’ingrédient actif l’ingrédient non actif étant chimiquement lié à l’ingrédient actif, p. ex. conjugués polymère-médicament le conjugué étant caractérisé par sa forme physique ou sa forme galénique, p. ex. émulsion, particule, complexe d’inclusion, stent ou kit
A61K 51/10 - Anticorps ou immunoglobulinesLeurs fragments
C07D 257/02 - Composés hétérocycliques contenant des cycles comportant quatre atomes d'azote comme uniques hétéro-atomes du cycle non condensés avec d'autres cycles
C07K 7/06 - Peptides linéaires ne contenant que des liaisons peptidiques normales ayant de 5 à 11 amino-acides
C07K 7/08 - Peptides linéaires ne contenant que des liaisons peptidiques normales ayant de 12 à 20 amino-acides
NATIONAL UNIVERSITY CORPORATION KAGOSHIMA UNIVERSITY (Japon)
NATIONAL UNIVERSITY CORPORATION GIFU UNIVERSITY (Japon)
Inventeur(s)
Suda, Yasuo
Wakao, Masahiro
Ishida, Hideharu
Yuki, Nobuhiro
Abrégé
Sugar-chain-immobilized fluorescent nanoparticles that allow quick and convenient detection of ganglioside-binding autoantibodies in blood serum from immune-mediated peripheral neuropathy patients are provided, as is a use for said sugar-chain-immobilized fluorescent nanoparticles. These sugar-chain-immobilized fluorescent nanoparticles contain the following: sugar-chain ligand complexes comprising sugar chains, including ganglioside-derived sugar chains, and a prescribed linker compound that has a hydrocarbon chain or the like on the main chain thereof; and fluorescent nanoparticles that have a prescribed core-shell structure. These sugar-chain-immobilized fluorescent nanoparticles are obtained by immobilizing the abovementioned sugar chains.
National University Corporation Kagoshima University (Japon)
EZAKI GLICO CO., LTD. (Japon)
Inventeur(s)
Kadokawa, Junichi
Takaha, Takeshi
Kubo, Akiko
Yanase, Michiyo
Hosoya, Kayo
Abrégé
Disclosed is an uronic acid-containing glucan or a modified product thereof. Specifically disclosed is a glucuronic acid-containing glucan in which a glucuronic acid residue is bound to at least one non-reducing terminal of a glucan, wherein the glucan is branched α-1,4 glucan or linear α-1,4 glucan. The glucuronic acid-containing glucan can be produced by allowing α-glucan phosphorylase derived from Aquifex aeolicus VF5 to act on glucuronic acid-1-phosphate to thereby transfer a glucuronic acid residue to the non-reducing terminal of the receptor glucan.
National University Corporation Kagoshima University (Japon)
Inventeur(s)
Kadokawa junichi
Takaha takeshi
Hosoya kayo
Abrégé
A graft polymer in which an α-1,4-glucan side chain is bonded to the main chain of cellulose: wherein the terminal carbon atom at the 1-position of the α-1,4-glucan side chain is covalently bonded via an –NH- group to the carbon atom at the 6-position in at least one glucose residue of the cellulose main chain; two hydrogen groups are bonded to the preceding carbon atom at the 1-position or one oxygen atom is bonded thereto; the preceding cellulose main chain has a degree of polymerization of 25 or higher; and the preceding α-1,4-glucan side chain has a degree of polymerization of 25 or higher.
C08B 15/06 - Dérivés contenant des éléments autres que carbone, hydrogène, oxygène, halogènes ou soufre contenant de l'azote
9.
Sugar-immobilized metal nanoparticle, method for measuring sugar-protein interaction using the same and method for recovering protein from sugar-protein interactant
National University Corporation Kagoshima University (Japon)
Inventeur(s)
Suda, Yasuo
Nishimura, Tomoaki
Kishimoto, Yuko
Nakagawa, Hiromi
Abrégé
It is intended to provide a stable novel sugar-immobilized metal nanoparticle capable of easily immobilizing a sugar chain, a method for measuring sugar-protein interaction easily and at a low cost using the same without labeling, and a method for simply recovering a protein from a sugar-protein interactant. A maltose-immobilized gold nanoparticle was obtained by binding a ligand complex, in which maltose and a linker compound had been bound to each other, to a gold nanoparticle. By adding this maltose-immobilized gold nanoparticle to a dilution series of concanavalin A, a sugar-protein interactant of maltose and ConA was formed, and red-purple color derived from a colloidal solution of maltose-immobilized gold nanoparticle disappeared. That is, sugar-protein interaction could be confirmed by visual observation without labeling.
A01N 43/04 - Biocides, produits repoussant ou attirant les animaux nuisibles, ou régulateurs de croissance des végétaux, contenant des composés hétérocycliques comportant des cycles avec un ou plusieurs atomes d'oxygène ou de soufre comme uniques hétéro-atomes du cycle avec un hétéro-atome
A61K 31/715 - Polysaccharides, c.-à-d. ayant plus de cinq radicaux saccharide liés les uns aux autres par des liaisons glycosidiquesLeurs dérivés, p. ex. éthers, esters
G01N 33/00 - Recherche ou analyse des matériaux par des méthodes spécifiques non couvertes par les groupes
National University Corporation Kagoshima University (Japon)
Inventeur(s)
Suda, Yasuo
Abrégé
A novel ligand conjugate which is effectively utilizable for analyzing a function of a protein; a ligand-supporting object; and a method of analyzing a protein. The ligand conjugate has a structure which comprises: a linker compound having a structure represented by the following General Formula (1):
(wherein n and p each is an integer of 0 to 6) in which X is a structure comprising one, two, or three hydrocarbon derivative chains which have an aromatic amino group at the end and may have a carbon-nitrogen bond in the main chain, Y is a hydro-carbon structure containing one or more sulfur atoms, and Z is a straight-chain structure comprising a carbon-carbon bond or carbon-oxygen bond; and a sugar which has a reducing end and is bonded to the linker compound through the aromatic amino group.
G01N 33/53 - Tests immunologiquesTests faisant intervenir la formation de liaisons biospécifiquesMatériaux à cet effet
G01N 33/532 - Production de composés immunochimiques marqués
G01N 33/553 - Support métallique ou recouvert d'un métal
11.
NOVEL SUGAR-IMMOBILIZED METAL NANOPARTICLE, METHOD FOR MEASURING SUGAR-PROTEIN INTERACTION USING THE SAME AND METHOD FOR RECOVERING PROTEIN FROM SUGAR-PROTEIN INTERACTANT
NATIONAL UNIVERSITY CORPORATION KAGOSHIMA UNIVERSITY (Japon)
Inventeur(s)
Suda, Yasuo
Nishimura, Tomoaki
Kishimoto, Yuko
Nakagawa, Hiromi
Abrégé
It is intended to provide a stable novel sugar-immobilized metal nanoparticle capable of easily immobilizing a sugar chain, a method for measuring sugar-protein interaction easily and at a low cost using the same without labeling, and a method for simply recovering a protein from a sugar-protein interactant. A maltose-immobilized gold nanoparticle was obtained by binding a ligand complex, in which maltose and a linker compound had been bound to each other, to a gold nanoparticle. By adding this maltose-immobilized gold nanoparticle to a dilution series of concanavalin A, a sugar-protein interactant of maltose and ConA was formed, and red-purple color derived from a colloidal solution of maltose-immobilized gold nanoparticle disappeared. That is, sugar-protein interaction could be confirmed by visual observation without labeling.
G01N 33/543 - Tests immunologiquesTests faisant intervenir la formation de liaisons biospécifiquesMatériaux à cet effet avec un support insoluble pour l'immobilisation de composés immunochimiques
C07K 1/22 - Chromatographie d'affinité ou techniques analogues basées sur des procédés d'absorption sélective
G01N 33/553 - Support métallique ou recouvert d'un métal
12.
SUGAR CHAIN LIGAND COMPOSITE AND METHOD OF ANALYZING PROTEIN WITH THE LIGAND COMPOSITE
NATIONAL UNIVERSITY CORPORATION KAGOSHIMA UNIVERSITY (Japon)
Inventeur(s)
Suda, Yasuo
Abrégé
A novel ligand conjugate which is effectively utilizable for analyzing a function of a protein; a ligand-supporting object; and a method of analyzing a protein. An aspect of the present invention provides a ligand conjugate having a linker compound and a sugar, the linker compound having a structure represented by General Formula (1): (see formula 1) where p and q are independently integers of not less than 0 but not more than 6, in which X is a structure comprising one, two, or three hydrocarbon derivative chains which have an aromatic amino group at an end and may have a carbon-nitrogen bond in a main chain, Y is a sulfur atom or a hydrocarbon structure containing a sulfur atom, and Z is a straight-chain structure comprising a carbon-carbon bond or carbon-oxygen bond, the sugar chain being selected from group (101). The sugar having a reducing end and being bonded to the linker compound through the aromatic amino group.