18 results about "Gln - Glutamine" patented technology

Disclosed are azotomycin prodrugs their use in treating diseases, disorders, or conditions associated with excess and / or aberrant glutamine utilization, including cancer.

The application discloses a novel double-carrier expression system for protein expression and a construction method and application thereof. The novel double-carrier expression system for protein expression comprises a first carrier containing a nucleotide sequence for coding a first functional domain of glutamine synthetase and a nucleotide sequence of light chain and heavy chain of a protein to be expressed; and a second carrier containing a nucleotide sequence for coding a second functional domain of glutamine synthetase and a nucleotide sequence of a ScFv sequence of the protein to be expressed, and an amino acid sequence of the glutamine synthetase is composed of the first functional domain and the second functional domain. By using the expression system, the transfection efficiency and screening efficiency are greatly improved, and the expression amount of the target protein is obviously increased.

1. Name of the designed product: packing bottle (glutamine powder). 2. Use of the designed product: the designed product is used for packing health-care food. 3. Design points of the designed product: combination of shape and pattern. 4. Picture or photo best indicating the design points: front view.

An object of the present application is to provide a new composition for promoting ketogenesis. According to the present application, there is provided a composition for promoting ketogenesis containing one or two or more amino acids selected from the group consisting of citrulline, leucine, cysteine, taurine, glutamine and aspartic acid. The composition of the present application can further contain either or both of a medium-chain fatty acid and a medium-chain fatty acid ester.

This invention discloses a method for constructing a Brca2-p.Q462Ter genetically engineered mouse and its application. The Brca2 genetically engineered mouse provided by this invention carries a truncated mutation in its Brca2 gene. This mutation is located at exon 10 of the mouse Brca2-201 transcript, changing amino acid position 462 from glutamine Q (Gln) to the stop codon Ter, forming the Brca2-p.Q462Ter mutation. The Brca2-p.Q462Ter genetically engineered mouse is used to simulate the human BRCA2 gene truncated mutation p.Gln472Ter, c.1414C>T. Amino acid homology analysis shows that the mouse BRCA2 protein Q462 site is homologous to the human BRCA2 protein Q472 site; therefore, this mouse mutation site can be used to simulate the corresponding truncated mutation effect in human BRCA2. This genetically engineered mouse can simulate, at the whole animal level, the abnormal DNA damage repair, impaired homologous recombination repair function, decreased genome stability, and susceptibility to related diseases caused by BRCA2 truncated mutations, thus providing a reliable tool for research on BRCA2-related pathogenesis, developmental effects, drug screening, and efficacy evaluation.

Provided is a method of selecting a camelid nanobody from a library of camelid nanobody sequences collected from B cells from a camelid immunized with an antigen. The method comprises: (a) identifying a camelid nanobody that has at least one of the following features (i) a phenylalanine (F) at position 42 (IMGT numbering); (ii) a short hinge; (iii) two or more cysteines in the nanobody sequence; (iv) a glutamine (Q) at position 123 (IMGT numbering); (v) low immunogenicity metric; (vi) non-classic VHH derived from germline IGHV3 or a valine (V) at position 42 (IMGT numbering); (vii) non-classic VHH derived from germline IGHV4 or an isoleucine (I) at position 42 (IMGT numbering); (viii) a histidine (H), aspartic acid (D) or glutamic acid (E) in the CDR region; (ix) a histidine (H), aspartic acid (D) or glutamic acid (E) in the first three amino acid residues, the FR2 region, or the first sixteen amino acid residues of the FR3 region of the nanobody sequence; (x) a tyrosine (Y) at position 42 (IMGT numbering), and the nanobody having a loop, concave paratope structure configuration; or (xi) a phenylalanine (F) at position 42 (IMGT numbering), and the nanobody having a convex paratope structure configuration; and (b) measuring one or more biological activities of the nanobody identified in step (a).

A method for differentiating non-human primate iPSCs into neurons may include providing a modified vector containing a piggyBac vector backbone, the modified vector expressing differentiation factor genes; treating the non-human primate iPSCs in a culture medium with the modified vector; replacing the culture medium with a second culture medium comprising BDNF, NT-3, and laminin; adding a culture medium supplemented with L-glutamine or an L-glutamine substitute, BDNF, and NT3; and generating neuronal lineage cells.

The application provides a pH-responsive acidifier-essential oil composite nanoemulsion, a preparation method and application thereof, and belongs to the field of poultry feed additives. The composite nanoemulsion comprises the following components in parts by mass: 10-15 parts of a composite acidifier, 3-5 parts of essential oil, 1-3 parts of glutamine, 1-2 parts of fructooligosaccharide, 4-8 parts of triglyceride prepared from a fatty acid with a carbon chain length of C8-C12, 12-18 parts of a surfactant, 8-12 parts of an alcohol solvent, and 40-50 parts of deionized water; the composite acidifier is composed of formic acid, propionic acid and coated phosphoric acid in a mass ratio of (2-4):(1-3):(4-6), the coated phosphoric acid is obtained by coating phosphoric acid with glycerol monostearate; and the essential oil is a mixture of cinnamaldehyde and oregano oil. The composite nanoemulsion can replace antibiotics when added to poultry basic feed, improve the daily weight gain of poultry, and reduce the feed conversion ratio and the diarrhea rate.

The present invention relates to a detoxifying peptide, characterized in that its sequence comprises the following general amino acid sequence: N-(Val-Gly-X1-X2-Pro-Gly)n-OH, in which: N and OH correspond respectively to the N-terminal and C-terminal end of the peptide; X1 and X2 are chosen from valine (Val), glycine (Gly), threonine (Thr), asparagine (Asn), glutamine (Gln), alanine (Ala), leucine (Leu) and isoleucine (Ile); n is an integer between 1 and 3; for use in the treatment and / or prevention of a disorder associated with glycation and / or glycoxidation of proteins and / or lipids.

This invention discloses a modified American cockroach polypeptide derivative, its preparation method, polypeptide composition, and applications. The amino acid sequence of the polypeptide derivative is shown in SEQ ID NO: 1 (PA1702); it is modified by replacing the asparagine at position 13 of the natural polypeptide PA1701 with glutamine, and can be prepared by Fmoc solid-phase polypeptide synthesis. Network pharmacology predicts that it acts on 59 core anti-inflammatory targets, enriched in pathways such as PI3K-Akt and MAPK. Molecular docking shows that PA1702 has a strong binding affinity for TNF-α and AKT1. In vitro experiments confirm that PA1702 is non-cytotoxic, can inhibit LPS-induced release of NO, TNF-α, IL-6, and IL-1β, and promote cell migration. The above-mentioned polypeptide derivative can be used as an active ingredient in cosmetics or pharmaceutical compositions; it has anti-inflammatory, skin barrier repair, and wound healing promotion effects, and can be used to prepare anti-inflammatory, skin barrier repair, and wound healing-promoting cosmetics or drugs.

The application discloses a gel factor and a preparation method and application thereof. A structural formula of the gel factor is shown in the following formula: wherein R1 is a side chain group except for an amino group, a carboxyl group and one hydrogen atom connected to a central carbon atom of an amino acid, and the amino acid is selected from one of glycine, alanine, valine, leucine, isoleucine, methionine, proline, tryptophan, serine, tyrosine, cysteine, phenylalanine, asparagine, glutamine, threonine, aspartic acid, glutamic acid, lysine, arginine, histidine and selenocysteine; R2 is an alkyl group with 16-19 carbon atoms; and R3 is a 9-fluorenylmethyloxy carbonyl group or a tert-butyloxy carbonyl group. The gel factor has a hydrophobic long alkyl tail chain, can spontaneously aggregate and assemble into a three-dimensional network structure through hydrogen bonds, pi-pi interaction and hydrophobic force, and can effectively fix oil solvents or oil phases in oil-water mixtures to form a high-strength gel.

This peptide, or a pharmaceutically acceptable salt thereof, contains a substructure having an amino acid sequence selected from the group consisting of (1) and (2). (1) Amino acid sequence represented by formula (I): RYRYYGHNLIAYGFY (SEQ ID NO: 1); (2) Amino acid sequence represented by formula (I) with 1 to 6 amino acids substituted, where, when the arginine at the N terminus is defined as the first amino acid residue, the first amino acid residue is optionally substituted with a basic amino acid other than arginine and histidine; the second amino acid residue is optionally substituted with an aromatic amino acid other than tyrosine and histidine; the third amino acid residue is optionally substituted with a basic amino acid other than arginine and histidine; the fourth amino acid residue is optionally substituted with an aromatic amino acid other than tyrosine and histidine; the fifth amino acid residue is optionally substituted with an aromatic amino acid other than tyrosine and histidine or an amino acid containing a hydroxy group; the sixth amino acid residue is optionally substituted with alanine or an analog thereof, or a glycine analog; the seventh amino acid residue is optionally substituted with an amino acid other than cysteine, lysine, proline, arginine, threonine, valine, and tryptophan; the eighth amino acid residue is optionally substituted with aspartic acid, glycine, tyrosine, phenylalanine, serine, histidine, glutamic acid, glutamine, alanine, leucine, or analogs thereof, or an asparagine analog; the ninth amino acid residue is optionally substituted with an amino acid other than glycine, proline, and tryptophan; the tenth amino acid residue is optionally substituted with a branched chain amino acid other than isoleucine; the eleventh amino acid residue is optionally substituted with an amino acid other than glycine, proline, and tryptophan; the twelfth amino acid residue is optionally substituted with a tyrosine analog or a phenylalanine analog; the thirteenth amino acid residue is optionally substituted with alanine or an analog thereof, or a glycine analog; the fourteenth amino acid residue is optionally substituted with histidine, leucine, tyrosine, tryptophan, or analogs thereof, or a phenylalanine analog; and the fifteenth amino acid residue is optionally substituted with an aromatic amino acid other than tyrosine and histidine.

The application discloses a method for preparing dibutyl lauroyl glutamine and application, wherein long-chain alkyl acyl glycine and acetic anhydride are added into a first reaction container containing cyclohexane, a long-chain alkyl cyclization product is prepared by warming and refluxing reaction; the prepared long-chain alkyl cyclization product is added into a second reaction container containing cyclohexane, an alkaline substance and N-butyl acrylamide are further added for reaction, the alkaline substance and solvent are removed after the reaction, and a long-chain alkyl butylamide propenyl oxazolone is prepared; the prepared long-chain alkyl butylamide propenyl oxazolone is put into a third reaction container containing cyclohexane, n-butylamine is further added into the third reaction container for refluxing reaction, and the solvent is evaporated to prepare long-chain alkyl glutamic acid dibutylamide. The application firstly performs ring-closing reaction, then performs Michael addition on a reserved site of the structure, and ingeniously performs chain extension reaction on the structure, and finally obtains a target compound.

The invention belongs to the technical field of biomedical materials, and particularly relates to a targeted NPY polypeptide nuclide ligand as well as a preparation method and application thereof. The structural formula of the targeted NPY polypeptide nuclide ligand is as shown in formula (1), wherein L is a metal chelating agent. The preparation method comprises the following steps: (1) adding tyrosine, an activating agent, a condensing agent and a solvent into Rink Amide MBHA Resin, reacting at room temperature for 1-5 hours, and grafting tyrosine on the Rink Amide MBHA Resin; (2) adding arginine, an activating agent, a condensing agent and a solvent, reacting at room temperature for 1-5 hours, grafting arginine, and sequentially grafting glutamine, arginine, tryptophan, isoleucine, proline, asparagine, asparagine, tyrosine, histidine, arginine and a metal chelating agent according to the steps, so as to obtain polypeptide resin L-Arg-His-Tyr-Asp-Asp-Pro-Iso-Try-Arg-Gln-Arg-Tyr-Rink Amide MBHA Resin; and (3) adding the obtained polypeptide resin into a lysis solution, and reacting at room temperature for 1-5 hours to obtain the targeted NPY polypeptide nuclide ligand with good in-vivo and in-vitro stability.

This invention relates to an amino acid ester acyltransferase mutant, its encoding gene, and its application in the synthesis of glutamic-alanine dipeptide. Compared with existing technologies, the amino acid ester acyltransferase mutant disclosed in this invention exhibits high activity, high substrate concentration tolerance, and high selectivity for glutamic-alanine dipeptide synthesis / hydrolysis. In the application of catalyzing the condensation of L-alanine methyl ester and L-glutamine to prepare glutamic-alanine dipeptide, it demonstrates significant advantages in terms of high yield and high space-time yield. Compared with chemical synthesis methods, the synthesis of glutamic-alanine dipeptide using this enzyme does not require group protection and deprotection, the process is simple, the reaction conditions are mild, and the process is environmentally friendly, showing promising application prospects in the industrial production of glutamic-alanine dipeptide.

The invention relates to means and methods for the treatment of diseases involving autophagy by cells, which process according to the invention is involved in mechanisms of tissue repair, vascular permeability and immune responses. The invention provides methods and means to target the elastin receptor complex specifically and to provide molecules and compositions comprising a specific targeting agent as well as amino acid compositions that are involved in the pathway of autophagy and the diseases related thereto. The disclosure also relates to peptide-drug development, in particular to (the improvement of) autophagy inhibiting amino acid containing peptides, more in particular glutamine-containing peptides and / or glutamine and other autophagy modulating amino acid containing compositions useful in the treatment of vascular and inflammatory conditions. The invention further relates to the improvement of glutamine peptides useful in the treatment of diabetic, vascular and / or inflammatory conditions. The invention provides a Q- ER peptide, comprising a synthetic peptide or functional analogue thereof provided with at least one PG-domain amino acid motif xGxxPG or functional equivalent thereof, said PG- domain motif allowing targeting of said peptide to the elastin receptor complex (ER), wherein at least one amino acid at position x is selected from the group of amino acids alanine (in one letter code: A), glutamine (Q), glycine (G), valine (V), leucine (L), isoleucine (I), proline (P) and arginine, said peptide provided with at least one glutamine (Q).

A therapeutic composition comprising: L-arginine at 40% w / w; a branched-chain amino acid complex (BCAA) at 25% w / w, wherein the BCAA complex consists of leucine, isoleucine, and valine in a 2:1:1 ratio; L-glutamine at 15% w / w; myo-inositol at 10% w / w; one or more excipients containing fructose and flavorings at 10% w / w; and one or more micronutrients containing coenzyme Q10, folic acid, and zinc, or pharmaceutically acceptable salts thereof, in a total amount of less than 1% w / w, wherein the composition is configured to support cellular metabolism and reproductive function.

This invention discloses a daidzein reductase mutant and its application in the preparation of (S)-equorol. The amino acid sequence of the daidzein reductase mutant I53G / Q148M / Y182F is the amino acid sequence shown in SEQ ID NO: 2, with isoleucine at position 53 mutated to glycine, glutamine at position 148 mutated to methionine, and tyrosine at position 182 mutated to phenylalanine. The nucleotide sequence of the daidzein reductase mutant gene is shown in SEQ ID NO: 3. This gene was introduced into *E. coli* to obtain a recombinant genetically engineered bacterium containing this gene, enabling the preparation of a recombinant daidzein reductase mutant for the highly active and stereoselective reduction of daidzein to dihydrodaidzein, laying the foundation for the subsequent efficient bioprocessing of (S)-equorol.