117 results about "Amino acid peptide" patented technology

A class of 2′-fluoro-nucleoside compounds are disclosed which are useful in the treatment of hepatitis B infection, hepatitis C infection, HIV and abnormal cellular proliferation, including tumors and cancer. The compounds have the general formulae:

wherein

• [0001]
  • Base is a purine or pyrimidine base;
  [0002]
  • R¹ is OH, H, OR³, N₃, CN, halogen, including F, or CF₃, lower alkyl, amino, loweralkylamino, di(lower)alkylamino, or alkoxy, and base refers to a purine or pyrimidine base;
  [0003]
  • R² is H, phosphate, including monophosphate, diphosphate, triphosphate, or a stabilized phosphate prodrug; acyl, or other pharmaceutically acceptable leaving group which when administered in vivo, is capable of providing a compound wherein R² is H or phosphate; sulfonate ester including alkyl or arylalkyl sulfonyl including methanesulfonyl, benzyl, wherein the phenyl group is optionally substituted with one or more substituents as described in the definition of aryl given above, a lipid, an amino acid, peptide, or cholesterol; and
  [0004]
  • R³ is acyl, alkyl, phosphate, or other pharmaceutically acceptable leaving group which when administered in vivo, is capable of being cleaved to the parent compound, or a pharmaceutically acceptable salt thereof.

Endothelial cell attachment to an intravascular stent is promoted by coating the stent with an endothelial cell specific adhesion peptide. Coating is preferably carried out by activating the intravascular stent using plasma glow discharge, applying on the stent a layer or plurality of layers of a polymer such as poly(2-hydroxyethylmethacrylate), applying a tresylation solution containing pyridine and tresyl chloride, and applying a five amino acid peptide having the sequence glycine-arginine-glutamic acid-aspartic acid-valine.

The present invention provides compounds of the formula X—R¹-D-[Dpr, Orn or Lys](A)-R²(Z)-D-[Dpr, Orn or Lys](B)—R³(Y)—NR⁴R⁵; or R¹(X)-D-[Dpr, Orn or Lys](A)-R²(Z)-D-[Dpr, Orn or Lys](B)—R³(Y)—NR⁴R⁵, in which X is a hard acid cation chelator, a soft acid cation chelator or Ac—, R¹, R² and R³ are independently selected from a covalent bond or one or more D-amino acids that can be the same or different, Y is a hard acid cation chelator, a soft acid cation chelator or absent, Z is a hard acid cation chelator, a soft acid cation chelator or absent, and A and B are haptens or hard acid cation chelators and can be the same or different, and R⁴ and R⁵ are independently selected from the group consisting of hard acid cation chelators, soft acid cation chelators, enzymes, therapeutic agents, diagnostic agents and H. The present invention also provides methods of using these compounds and kits containing the compounds.

The invention provides methods, reagents and kits for amino acid, peptide and protein identification, differential quantitation and for the analysis of post translational modification and cross-linking status, comprising: derivatizing a mixture of amino acids peptides or proteins, to form at least one amino acid peptide or protein containing a fixed-charge ion, other than at the C-terminal or N-terminal end thereof; introducing the mixture of amino acids peptides or proteins containing the fixed charge derivatized amino acid peptide or protein to a mass spectrometer; passing the mixture of amino acids peptides or proteins containing the fixed charge derivatized amino acid peptide or protein through a first mass resolving spectrometer to select precursor protein or peptide ions having a first desired mass-to-charge ratio; subjecting the precursor ions of the first mass to charge ratio to dissociation to form a product ion having a second mass-to-charge ratio that is characteristic of a fragmentation occurring at a site adjacent to the fixed charge; and detecting the product ions having the second mass-to-charge ratio. The product ion having the second mass-to-charge ratio may be either a product ion formed by neutral loss of the fixed charge from the precursor ion, or a product ion formed by charged loss of the fixed charge from the precursor ion.

The invented healthy edible salt is prepared by mixing with sodium chloride, various amino acid, peptide substance, vitamin B family, polysaccharide, or chitin, antioxidant, nucleic acid seasoning, potassium chloride, calcium salt, magnesium salt, selenium salt, and potassium iodide. It can effectively prevent various diseases, also can prevent osteoporosis, cancer, diabetes, dysinsulinosis, lithiasis, coronary heart disease, senile dementia, bark farus etc. it also possesses the functions of antisenility, antifatigue, antidepression, improving immune power, promoting growth etc.

This invention relates to compositions and methods of delivering therapeutic agents to bone. More specifically, the invention relates to endowing a large molecule vectors i.e., adeno virus, retrovirus, liposomes, micelles, natural and synthetic polymers, or combinations thereof, with the ability to target bone tissue in vivo and with improved stability in the blood, by attaching multiple copies of acid amino acid peptides. One preferred embodiment of the invention relates to endowing an adeno-associated virus (AAV) vector with the ability to target bone-tissue in vivo and improve its stability, by the addition of multiple acidic amino acid peptides attached to the capsid of the viral vector.

The invention discloses a preparation method of liraglutide, and belongs to the technical field of medicines. The method comprises the following steps of (1) carrying out solid-phase synthesis to form four peptide segments of the liraglutide, wherein the peptide segment 1 is the (1-9)th amino acids in a liraglutide main chain sequence, the peptide segment 2 is the (10-14)th amino acids in the liraglutide main chain sequence, the peptide segment 3 is the (15-23)th amino acids in the liraglutide main chain sequence and the peptide segment 4 is the (24-31)th amino acids in the liraglutide main chain sequence; (2) stepwise coupling various peptide segments to obtain an all-protected liraglutide main chain peptide; (3) removing a protecting group of the 20th lysine and completing connection of side chains to obtain all-protected liraglutide peptide resin; and (4) carrying out cracking, purification and freeze-drying to obtain the liraglutide. The preparation method is high in production efficiency and stable in process, and a product is high in purity, high in yield and suitable for industrial production.

A bamboo root amino-acid peptide extract, its production and use are disclosed. The extract contains amino acid 10-50wt%, which consists of free amino acid 5-40wt%, tyrosine, serine, aspartine, glutamic acid, alanine, phenylalaine, valine and delta-OH-Lys. It has good taste and can be used for functional food, beverage and condiment.

Disclosed is a process for preparing 5-peptide product, which comprises obtaining arginine hydrolysate, proline hydrolysate, aspartate hydrolysate, leucine hydrolysate and lysine hydrolysate through complex enzyme decomposition, employing hyperfiltration membrane to separate and reclaim 5000-1000D liquids containing rich amino acid 5-peptide molecular structures such as praline, arginine, aspartate, lycine, and leucine, then carrying out desalination, decolorization, crystallizing, embedding and drying into fine powders.

The invention relates to antimicrobial cathelicidin polypeptides related to a 38 amino acid peptide having SEQ ID NO:4. The invention provides for polypeptides having broad spectrum antimicrobial activity, nucleic acids and expression vectors encoding such polypeptides, as well as host cells and methods of reducing survival of a microbe. In addition, the invention also provides compositions, as well as articles of manufacture, that comprise a broad spectrum antimicrobial polypeptide.

A solid phase assay is used for detecting antibodies to INGAP^104-118 peptide, a 15-amino acid peptide that is the biologically active portion of islet neogenesis associated protein (INGAP). The isotype of the antibodies to INGAP^104-118 peptide can be determined. A kit can also be used in the detection of anti-INGAP^104-118 antibodies. Endogenous autoantibodies or antibody production during therapeutic treatment of a mammal with INGAP^104-118 can be monitored.

This invention relates to a cTnI monocloned antibody and its hybridoma cell system. The said monocloned antibody has high specificity sensitivity and is easily prepared. It can identify different antigenic determinants on amino acid peptide segments 28-42, so as to be used for preparation of kits for diagnosis of cardiac infarction, angina pectoris and myocarditis.

The invention provides D02S derivatives conjugated to monosaccharide ligands directly or through a linker and optionally chelated to a metal, wherein the D02S derivatives having the following structure: wherein R₁′, R₂′ are each independently —OH or —O-alkyl; R₁ is a hydrogen, a linker, or a ligand; R₃ is a linker and/or a ligand; and n is an integer from 1 to 10; the linker is an amino acid, a peptide, an amino alcohol, a polyethylylene glycol, an alkyl, an alkenyl, an alkynyl, an azide, an aromatic compound, a carboxylic acid, or an ester, the alkyl, alkenyl, or alkynyl is optionally substituted with an alkyl, a halogen, a nitro group, a hydroxyl group, an amino group, or a carboxyl group; the ligand is a GLUT1 targeting moiety.

It is an object of the present invention to provide a luminescent polymer that is useful as a luminescent signal probe for labeling and detecting a target substance at high sensitivity in bioassay, and to provide the application of said luminescent polymer to bioassay. The luminescent polymer of the present invention comprises at least one biotin covalently attached to a polymer that includes monosaccharide or amino acid as a constituent monomer covalently attached to a luminescent substance. Preferably, two or more biotins are attached. Examples of the above-mentioned luminescent substance include cyanoisoindoles, luminols, and acridinium esters, and examples of the polymer include polysaccharides, polyamino acids, peptides, polypeptides, and proteins.

Disclosed are methods of isolating linaclotide, a cyclized 14-amino-acid peptide with three disulfide bonds. The sequence consists of Cys-Cys-Glu-Tyr-Cys-Cys-Asn-Pro-Ala-Cys-Thr-Gly-Cys-Tyr with disulfide bridges between the cysteine residues at positions 1 and 6, 2 and 10, and 5 and 13. The drug acts as a GCC superagonist, elevating intracellular cGMP composition for treating various disorders, including gastrointestinal disorders, obesity, congestive heart failure and benign prostatic hyperplasia.

The invention discloses a preparation method and application of a pullulanase mutant PulB-d99-D436H. The preparation method comprises the steps that 100-926 amino acid peptide fragments of bacillus naganoensis pullulanase are cut, aspartic acid (Asp) at the 436 locus of the amino acid peptide fragments is mutated into histidine (His), and then the novel pullulanase mutant is obtained through transformation. The preparation method and application of the pullulanase mutant PulB-d99-D436H have the advantages that the mutant enzyme has the excellent characteristics compared with an enzyme before mutation, wherein the enzyme expression quantity is 3.8 times of that of a parent enzyme, the optimum temperature is increased by 2.5 DEG C, and the catalytic activity is 1.36 times of that of the parent enzyme. The mutant gene is integrated into chromosomes of bacillus subtilis to construct and recombine the bacillus subtilis, and therefore pullulanase can be stably fermented and produced. The hydrolysis efficiency of starch and pullulan can be improved through the mutant enzyme.

Specific drug delivery to tumor cells without affecting normal cells is a major challenge in cancer treatment. The present invention incorporates embedding nonionic surfactant vesicles (niosomes) containing an anti-cancer therapeutic agent with chlorotoxin into a thermosensitive chitosan hydrogel network. Chitosan has mucoadhesive property which can be used in the targeting of the tumor cells with the mucin over expression. Chlorotoxin is a 36 amino acid peptide obtained from Leiurus quinquestriatus scorpion venom which binds preferentially to tumor cells of neuroectodermal origin but not to normal cells. The incorporation of chlorotoxin along with niosomes in the chitosan hydrogel is used as the second targeting strategy to further improve the specific delivery of drugs to tumor cells such as glioma.

A human urocortin-related peptide with significant sequence homology to the CRF neuropeptide family was identified. A mouse cDNA was isolated from whole brain poly (A+) RNA that encodes a predicted 38 amino acid peptide protein designated herein as urocortin II. Both human URP and mouse Ucn II are structurally related to the other known mammalian family members, CRF and urocortin (Ucn). These peptides are involved in the regulation of the hypothalamic-pituitary-adrenal axis under basal and stress conditions, suggesting a similar role for URP and Ucn II. Synthesized Ucn-II and URP peptide binds with higher affinity to CRF-R2 than to CRF-R1 Ucn II and human URP appear to be involved in the regulation of body temperature and appetite and may play a role in other stress related phenomenon. These findings identify Ucn II and human URP as a new members of the CRF family of neuropeptides, which are expressed centrally and bind to CRF-R2.