30 results about "Gelatinases" patented technology

The invention belongs to the technical field of metal nanomaterials, and particularly discloses an antibacterial nanoprobe BSA@AuNc-AMP-Ce6 and a preparation method and application thereof. An antibacterial peptide marked by Ce6 is connected to BSA@AuNc through an Au-S bond, and PLGVRG in a polypeptide sequence is a gelatinase enzyme digestion sequence and can be recognized and cut off by gelatinase secreted by S. aureus; the photosensitizer Ce6 is introduced for PDT antibiosis, and the photosensitizer Ce6 generates reactive oxygen species (ROS) under the irradiation of laser, so microbial molecules are oxidized and cells are damaged and die; and the photosensitizer Ce6 and antibacterial peptide (AMP) generate a synergistic effect. The antibacterial nanoprobe BSA@AuNc-AMP-Ce6 prepared by using the preparation method disclosed by the invention has more excellent antibacterial performance than traditional antibacterial peptides, and is good in biocompatibility, small in interference to normal physiological activities of body cells, low in toxicity and high in safety.

The invention relates to VHH (variable domain of heavy chain of heavy-chain antibody) antibody gene derived from anti-CyPA (CyclophilinA) animal of family Camelidae, encoded polypeptide, and application of the gene and the polypeptide in preparing drugs for treating inflammatory diseases such as rheumatoid arthritis. The VHH antibody gene has gene sequence shown in sequence table (400)1, the encoded polypeptide has amino acid sequence shown in sequence table (400)2. Lama pacos as immune animal is used, and phage display techniques (PDT) are adopted to successfully obtain an anti-CyPA VHH antibody capable of specifically combining with expressed CyPA antigen. The antibody can inhibit monocytes THP-1 chemotaxis and gelatinase secretion induced by CyPA. Dimer or polymer can be constructed by gene engineering method, to be applied in diagnosis or research on drugs for treating inflammatory diseases. The gene and the polypeptide establish foundation for further research on related drugs for treating rheumatoid arthritis.

The present invention relates to the use of Neutrophil Gelatinase-Associated Lipocalin (NGAL) and / or SERPINA3 as biomarkers of the Mineralocorticoid Receptor (MR) activation in a patient. More particularly, the present invention relates to a method for predicting the responsiveness of a patient to a treatment with a MR antagonist or an aldosterone synthase inhibitor, said method comprising determining in a biological sample obtained from said patient the expression level of the NGAL gene and / or of the SERPINA3 gene.

Matrix metalloproteinases (MMPs) are a group of enzymes that have been implicated in the pathological destruction of connective tissue and basement membranes. These zinc containing endopeptidases consist of several subsets of enzymes including collagenases, stromelysins and gelatinases. TNF-alpha converting enzyme (TACE), a pro-inflammatory cytokine, catalyzes the formation of TNF-alpha from membrane bound TNF-alpha precursor protein. It is expected that small molecule inhibitors of MMPs and TACE therefore have the potential for treating a variety of disease states. The present invention provides low molecular weight, non-peptide inhibitors of matrix metalloproteinases (MMPs) and TNF-alpha converting enzyme (TACE) for the treatment of arthritis, tumor metastasis, tissue ulceration, abnormal wound healing, periodontal disease, bone disease, diabetes (insulin resistance) and HIV infection having the formula wherein R2 and R3 form a heterocyclic ring and A is S, S(O), or S(O)2, and R1 and R4 are defined herein.

Provided herein are nanoparticles that include a lipid layer and a compartment surrounded by the lipid layer. The lipid layer may include a lipid and a lipoprotein. The lipid may include a POPE lipid covalently attached to a hydrophilic polymer by a disulfide bond. The lipoprotein may include a trigger protein. The concentration of the first lipid may be between 1 mol % and 30 mol %. The disulfide bond of the first lipid is stable under conditions that include 10% human serum and is broken under conditions that include 50 micromolar glutathione. The hydrophilic polymer may include a PEG molecule. The trigger protein may include an amino acid repeat region, such as (GPX)n. The trigger protein may include a peptide bond that is cleaved by a gelatinase (e.g., gelatinase-B protease), or a member of the ADAM family of proteases (e.g., ADAM10 protease). Also provided are methods of using the nanoparticles.

The invention discloses anti-inflammatory application of a small molecule compound AG-4, and application in preparing anti-inflammatory drug. The small molecule compound AG-4 is screened through a candidate drug screening platform combining structural biology, information biology and biological activity determination. The small molecule compound AG-4 can realize specific binding with CD147 protein to inhibit inflammatory cell chemotaxis and secretion of chemotaxis; the invention is also suitable for preparing medicines for treating CD147 protein high expression related diseases (such as rheumatoid arthritis).

The invention relates to VHH (variable domain of heavy chain of heavy-chain antibody) antibody gene derived from anti-CyPA (CyclophilinA) animal of family Camelidae, encoded polypeptide, and application of the gene and the polypeptide in preparing drugs for treating inflammatory diseases such as rheumatoid arthritis. The VHH antibody gene has gene sequence shown in sequence table (400)1, the encoded polypeptide has amino acid sequence shown in sequence table (400)2. Lama pacos as immune animal is used, and phage display techniques (PDT) are adopted to successfully obtain an anti-CyPA VHH antibody capable of specifically combining with expressed CyPA antigen. The antibody can inhibit monocytes THP-1 chemotaxis and gelatinase secretion induced by CyPA. Dimer or polymer can be constructed by gene engineering method, to be applied in diagnosis or research on drugs for treating inflammatory diseases. The gene and the polypeptide establish foundation for further research on related drugs for treating rheumatoid arthritis.

The invention belongs to the field of biological medicine, and particularly relates to a drug-loaded nanoparticle with a core-shell structure and a preparation method and application thereof.The nanoparticle is of a shell-core structure composed of gelatin nanoparticles, Cypate and fluorescently-labeled antibacterial peptide, A-type gelatin and a photothermal agent Cypate coupled with the A-type gelatin jointly form a nano shell, and Cy3-labeled antibacterial peptide (AMP-Cy3) serves as an embedded core. When the antibacterial peptide exists in a gelatinase microenvironment of an infected part, a gelatin shell is degraded, and the internal fluorescent antibacterial peptide is released in a responsive manner, so that the non-target toxicity of the antibacterial peptide is reduced. In addition, heat generated by the photothermal agent Cypate irradiated by near-infrared light can also provide a good bactericidal synergistic effect for the antibacterial peptide, so that the purpose of selectively and rapidly eradicating bacteria at an infected part is achieved. The composite nanoparticles are simple and convenient to synthesize, high in biocompatibility and excellent in bactericidal effect, and have potential clinical conversion value as an antibacterial agent.

The invention discloses a fluorescent polypeptide substrate for detecting human gelatinase MMP‑2. The fluorescent polypeptide substrate includes an amino acid sequence as shown in Peptide II, and the first valine in the amino acid sequence is bound to the fluorescent group 5-carboxyfluorescein, and the 11th lysine is bound to the fluorescent quenching group 5 ‑Carboxytetramethylrhodamine. The fluorescent polypeptide substrate of the present invention reacts with human MMP-2, and its enzymatic reaction kinetic constant Km is 315 μ M, Kcat / Km: 2565M ‑1 ·S ‑1 ; Human MMP-9 with an enzyme activity concentration of less than 6 μM has almost no reaction with the fluorescent polypeptide substrate of the present invention. The fluorescent polypeptide substrate for detecting human MMP-2 activity of the present invention does not react with the same family of human gelatinase MMP-9, and has certain specificity. The method for detecting human MMP-2 and screening human MMP-2 inhibitors of the present invention is simple and quick to operate and has good application prospects.

Methods for diagnosing renal disorders by measuring human neutrophil gelatinase-associated lipocalin (NGAL) are provided.