32 results about "Proteinase B" patented technology

The invention discloses a novel cathepsin B activation type targeted anti-tumor polypeptide m(KLA)-iRGD, the molecular weight is 2570, and the amino acid sequence is D(KLAKLAKKLAKLA)KGGCRGDKGPDC. The polypeptide is formed by KLA peptide and iRGD peptide through flexible connexon Gly-Gly. The sequence of the KLA peptide is KLAKLAKKLAKLAK, and amino acids of the KLAKLAKKLAKLA sequence at the N terminal of the polypeptide are all D-amino acids. The sequence of the iRGD peptide is CRGDKGPDC. The polypeptide has the advantage that the tumor targeted peptide iRGD and the apoptosis promoting peptide KLA are connected into the new polypeptide m(KLA)-iRGD for the first time. The polypeptide m(KLA)-iRGD can be specifically combined with alphaVbeta3 and NRP-1 receptors and enter tumor cells, mitochondrial apoptosis is initiated after the polypeptide is activated by intracellular cathepsin B (CTSB), tumor cells are selectively killed, and growth and migration of tumors are remarkably inhibited. Under the same concentration, a polypeptide m(KLA)-iRGD comparison peptide has higher tumor targeting and higher capacity of inhibiting tumor growth and migration. Meanwhile, the polypeptide m(KLA)-iRGD has no obvious toxicity on mouse weight and vital organs, and a solid foundation is laid for further clinical research and application.

The invention relates to a method for separating and purifying intestinal tract cathepsin B of a sea cucumber, which comprises the following steps: using sodium acetate buffer solution containing L-Cys to lixiviate a sea cucumber intestine homogenate breaking buffer solution at a temperature of 4 DEG C; adopting ammonia sulfate to perform fractional precipitation; using the sodium acetate buffer solution to dissolve the precipitate; and concentrating the dissolved precipitate after dialysis and demineralization to obtain crude enzyme of the cathepsin B. The crude enzyme of the cathepsin B is processed by 2 to 3 methods of ion exchange chromatography chromatogram, gel chromatogram and high-efficiency liquid chromatogram to achieve the aim of purification.

The invention discloses a chlorine-free and shrink-proof finishing technology of wool tops. The chlorine-free and shrink-proof finishing technology comprises the following steps: 1) washing with water: carrying out water-washing pre-treatment on the wool tops to remove impurities in the wool tops; 2) carrying out biological enzyme shrink-proof treatment: immersing the wool tops subjected to the water-washing treatment into a biological enzyme shrink-proof treatment solution; carrying out padding treatment, wherein the biological enzyme shrink-proof treatment solution is prepared from the following components in percentage by mass: 1 percent to 3 percent of hydrogen peroxide, 2 percent to 5 percent of sodium hydrogen sulfite, 15 percent to 20 percent of compound proteinase B, 35 percent to 40 percent of organic silicone resin, 7 percent to 10 percent of a penetrating agent and 29 percent to 33 percent of acrylic resin; 3) drying: drying the wool tops subjected to the biological enzyme shrink-proof treatment to obtain a wool top finished product with shrink-proof and anti-pilling performance. By adopting the manner, a technological flow is shortened so that the treated wool tops reach machine-washable shrink-proof effect of traditional chlorination and the anti-pilling performance is improved; in a finishing process, AOX (Absorbable Organic Halogen) pollution is not generated, and energy saving and environmental friendliness are realized.

A cathepsin B gene of bollworm and its clone and recombinant expression process are disclosed. Its preparing steps include extracting overall RNA from bollworm, reverse transcription to synthesize cDNA, designing primer, polymerase chain reaction, multiplication purifying, cloning it to pGEM-T Easy vector, transferring DH5 alpha cells for sequence test, fast multiplication to obtain end-to-end CDNA (1310 bp), and expressing proteinase in prokaryotic and eukaryotic organisms to generate cathepsin B with hydrolysis activity.

The invention provides a method for screening cathepsin B inhibitor by adopting ultra performance liquid chromatography and mass spectrometry. A cathepsin B inhibitor is a natural product extract or a monomer. The ultra performance liquid chromatography and mass spectrometry is used for analyzing the in vitro inhibition ratio of the natural product extract or monomer to a cathepsin B and the catalytic activity of the cathepsin B. The invention applies the ultra performance liquid chromatography and mass spectrometry to the screening of enzyme inhibitors, ensures rapid and accurate sample detection and the related coefficient of a linear equation of 0.997, adopts the mass spectrometry to detect a compound mass-charge ratio, has high accuracy and excellent specificity, avoids the false position and false negative results in a spectrometry screening, and can be used for the screening of the cathepsin B inhibitor and the kinetic study of the cathepsin B.

The invention belongs to the field of human hair product processing, and particularly relates to a bio-enzyme composite desquamation technology for human hair fiber. The bio-enzyme composite desquamation technology comprises a step of performing desquamation treatment on the human hair fiber sequentially through protease A and protease B, wherein the protease A is one of bacillus subtilis protease, bacillus licheniformis protease, bacillus cereus protease, ficin and chymotrypsin; and the protease B is one of actinomycetes protease, aspergillus oryzae, aspergillus niger, trypsin, endopeptidase, hemocoagulase, papain and bromelain. The technology provided by the invention is simple and easy to implement.

The invention provides polyamino acid. The polyamino acid is of a structure shown in the formula I (please see in the specification), wherein n is larger than or equal to 50 and smaller than or equal to 200, i is larger than or equal to 1 and smaller than or equal to 10, and j is larger than or equal to 3 and smaller than or equal to 30. One end of the polyamino acid is provided with hydrophilic methoxypolyethylene glycols, the other end of the polyamino acid is provided with a hydrophobic citrulline and valine copolymer, the amphiphilic polyamino acid with the hydrophilic chain section and the hydrophobic chain section can autonomously form micelle which is of a kernel-shell structure and has a nanometer size in water; chemical bonds between citrulline and valine of the polyamino acid can crack under the effect of cathepsin B, and therefore the polyamino acid can be degraded by enzymes, and the drug loaded micelle has high cathepsin B responsiveness. In addition, the drug loaded micelle has high biocompatibility and biodegradability.

The present invention provides a novel fluorine-containing <19>F nuclear magnetic resonance probe, which has a chemical formula of C49H58F6N10O7S3, has the following structural formula defined in thespecification, and can be used for detecting cathepsin B. According to the present invention, the magnetic resonance signal of the <19>F nuclear magnetic resonance probe is proportional to the activity of cathepsin B in vivo, the stronger the signal, the higher the activity of the cathepsin B, and the signal exceeding a certain threshold is related to malignant tumors, such that the new technicalway is provided for the early detection of tumors.

Prodrugs which can be activated by enzymes, are formulated for sequential administration, with enzyme conjugates. Either or each component comprises a polymeric carrier which allows it to be directed preferentially to the target tissue. A new polymer-prodrug conjugate is cleavable by Cathepsin B or other thiol-dependent protease. The invention is of particular utility for targeting solid tumours.

The invention relates to a double targeting hepatic tumor drug as well as a synthetic method and application thereof. The double targeting hepatic tumor drug has a terminal structure (galactose or N-acetyl galactose) capable of specifically binding to asialoglycoprotein receptor at the surface of a hepatocyte, and therefore the double targeting hepatic tumor drug is capable of binding to the asialoglycoprotein receptor so as to be brought into the interior of a hepatic tumor cell by means of the endocytosis of the hepatic tumor cell. On the other hand, experiments prove that the enzyme hydrolysis of the overexpressed cathepsin B in hepatic tumor cell lysosome is performed on the double targeting hepatic tumor drug to release Adriamycin, that is, active ingredients are released while the level of cathepsin B can be reduced, so as to slow down tumor progression. In summary, the double targeting hepatic tumor drug prepared by the invention uses asialoglycoprotein receptor and cathepsin Bas double target spots for having an effect, has obvious therapeutic effect, and meanwhile significantly reduces the toxic and side effects on other normal tissues and cells.

The invention belongs to the field of biomedicine, specifically relates to a docetaxel target prodrug and a pharmaceutical application thereof, and provides a novel docetaxel target prodrug represented by the formula (1) and an application thereof on preventing colorectal carcinoma. The provided compound has a pharmacology research value and can be used as an anti-cancer prodrug that targets the specific high expression of tumors of colorectal carcinoma. The prodrug can be used to treat colorectal carcinoma caused by specific high expression of one or more of matrix metalloproteinase MMP-7, cysteine cathepsin B, and fibroblast activator protein [alpha]. In the formula (1), A represents a substrate polypeptide sequence that can specifically identify and hydrolyze components that are obviously and highly expressed in tissues of colorectal carcinoma including but not limited to matrix metalloproteinase MMP-7, cysteine cathepsin B, and fibroblast activator protein [alpha]; B represents a degradable bridge connection group selected from (a to i) and is connected to the carbon end or nitrogen end of A through amido bonds; and R1 includes but not limited to a fluorine atom, a hydrogen atom, and the like.

Methods are provided for the production of gram to kilogram quantities of pro-EP-B2 (proenzyme form of EP-B2) in a lyophilized form. The methods include scalable fermentation, refolding and purification processes, which processes may be combined with lyophilization to yield a stable product.

The present invention provides methods for treating a subject afflicted with i) Mild Cognitive Impairment (MCI), ii) early dementia, iii) early α-synucleinopathy, iv) traumatic brain injury, v) cardiomyopathy, vi) eye disease, or vii) skin damage, comprising administering to the subject at least one compound that increases the level of active cathepsin B in cells of the subject, or a pharmaceutically acceptable salt or ester thereof, in an amount that is effective to treat the subject. The present invention also provides compositions for treating a subject afflicted with i) Mild Cognitive Impairment (MCI), ii) early dementia, iii) early α-synucleinopathy, iv) traumatic brain injury, v) cardiomyopathy, vi) eye disease, or vii) skin damage.

The invention discloses Agapanthus africanus cathepsin B, an encoding gene thereof, a probe and application. The Agapanthus africanus cathepsin B comprises protein (a) or protein (b), wherein the protein (a) is protein formed by an amino acid sequence as shown in SEQ ID No. 4; the protein (b) is protein which is obtained by subjecting the amino acid sequence as shown in SEQ ID No. 4 to substitution or deletion or by adding one or more amino acid to the amino acid sequence as shown in SEQ ID No. 4 and is derived from the protein (a), and the protein (b) has Agapanthus africanus ApCathB protein activity. The invention further provides a nucleotide sequence for encoding the protein and the probe for detecting the nucleotide sequence. The Agapanthus africanus cathepsin B, the encoding gene and the probe have the advantages that a foundation is laid for the further researches of enzyme properties and the expression level of the gene and the protein in various physiological and pathological states, the cathepsin B protein is obtained by the protein engineering technology, and the potential application prospect of the cathepsin B protein om tumor diagnosing and treating, agricultural disease and pest control, food and meat tendering and fragrance increasing, cell line separation and the like.

The present invention relates to a 2,3-epoxy succinyl derivative, a preparation method and a use thereof, in particular, the present invention relates to a compound represented by Formula (1), a racemate or an optical isomer thereof, a solvate thereof, or a pharmaceutically acceptable salt thereof. The compound according to the present invention has good inhibitory activity and/or selectivity against cathepsin, especially Cathepsin B, can be used in the treatment of multiple diseases associated with cathepsin, for example, osteoporosis, rheumatoid arthritis and osteoarthritis that are associated with Cathepsin K, Ebola virus infection, a degenerative disease and an autoimmune disease that are associated with Cathepsin L, S, especially Cathepsin B-related tumor diseases, such as gastric cancer, cervical cancer, lung cancer, breast cancer, prostate cancer, bladder cancer, colon cancer, neuroglioma, and melanoma.

The process of purifying and preparing cathepsin B inhibiting factor as one antitumor factor from soybean or soybean dregs includes grinding soybean or soybean dregs, stirring, precipitation, dialysis, exclusion chromatography and ion exchange column separation, elution, separate collection and other steps. The soybean cathepsin B inhibiting factor prepared through the process has obvious effect of inhibiting the growth of human cervical carcinoma cell (Hela) and neuroglioma cell (glioma). The present invention provides new way for developing new medicine and relevant health food for preventing and treating tumor and for deep processing of soybean product.

Epoxysuccinic acid derivatives having general formula (I): (wherein R<1> represents hydrogen, alkyl, aryl or aralkyl; R<2> and R<3> independently represent each aryl, aralkyl or alkyl; and X represents -O- or -NR<4>- wherein R<4> represents hydrogen, alkyl or aralkyl) is used in the prevention and treatment of bone diseases such as osteoporosis, malignant hypercalcemia, and bone Behcet's disease, in the treatment of osteoarthritis and rheumatoid arthritis in association with the abnormal hyperergasia of cathepsin L activity, and as a remedy for diseases in which cathepsins L and B participate such as muscular dystrophy and amyotrophy.

This invention relates to oxazolidine inhibitors of calpain and/or cathepsin B and to compositions containing them. As inhibitors of calpain and/or cathepsin B, the compounds are useful in the treatment of patients afflicted with acute or chronic neurodegenerative disorders.

The present invention relates to novel a-keto carbonyl calpain inhibitors for the treatment of neurodegenerative diseases and neuromuscular diseases including Duchenne Muscular Dystrophy, Becker Muscular Dystrophy and other muscular dystrophies. Disuse atrophy and general muscle wasting can also be treated. Diseases of the eye, in particular cataract, can be treated as well. Generally all condition where elevated levels of calpains are involved can be treated. The compounds of the invention may also inhibit other thiol proteases such as cathepsin B, cathepsin H, cathepsin L, papain or the like. Multicatalytic Protease also known as proteasome may also be inhibited and the compounds can therefore be used to treat cell proliferative diseases such as cancer, psoriasis, and restenosis. The compounds of the present invention are also inhibitors of cell damage by oxidative stress through free radicals can he used to treat mitochondrial disorders and neurodegenerative diseases, where elevated levels of oxidative stress are involved. In addition they induce the expression of utrophin, which is beneficial for the treatment of Duchenne Muscular Dystrophy and Becker Muscular Dystrophy.