1323results about "Connective tissue peptides" patented technology

The invention belongs to the field of biological materials, and particularly relates to recombinant V-type humanized collagen and application thereof. The invention provides a recombinant V-type humanized collagen, the amino acid sequence of the recombinant V-type humanized collagen comprises (repetitive unit) n, and the repetitive unit comprises a sequence as shown in SEQ ID NO.1; each repeating unit is directly linked and the number n of repeating units is 10. The recombinant V-type humanized collagen can comprehensively resist skin aging.

The invention relates to the technical field of biology, and particularly discloses a recombinant collagen III and application thereof in preparation of gel. The recombinant collagen III is designed by optimizing functional area sequences of human I-type and III-type collagen, the amino acid sequence is shown as SEQ ID No.2, and the recombinant collagen III has the characteristics of high stability, good hydrophilicity and low immunogenicity. The preparation method comprises the steps of expression vector construction, escherichia coli induced expression, affinity chromatography purification and renaturation. The recombinant collagen III can be prepared into a gel dressing and comprises sodium alginate, methylparaben and other components. Experiments show that the gel can effectively promote cell proliferation and has no cytotoxicity; in a mouse skin injury model, the collagen can relieve inflammation, accelerate wound healing and inhibit scar formation, and the effect of the collagen is superior to that of natural human III-type collagen. The invention provides a safe and efficient novel material for wound repair, and is suitable for medical dressings and tissue engineering.

The invention discloses a recombinant XVII type collagen engineering bacterium as well as a preparation method and application thereof, and belongs to the technical field of genetic engineering, and the recombinant XVII type collagen engineering bacterium is realized through three steps of designing and optimizing collagen, improving translation through codon optimization and selecting a vector for cloning. By optimizing the amino acid sequence and the codon, the expression efficiency and the stability of the recombinant XVII type collagen in engineering bacteria are improved. The optimization not only improves the production efficiency of the protein, but also reduces the production cost. The recombinant XVII type collagen has potential in the medical field, especially in the fields of skin repair, wound healing, aging resistance and the like. Meanwhile, in the fields of beauty and biological materials, collagen is widely applied to products such as masks and skin care products as a basic component, and can promote skin cell regeneration and enhance skin elasticity and repair capacity.

The invention relates to the technical field of synthetic biology, in particular to recombinant XVII type collagen as well as a preparation method and application thereof.The amino acid sequence of the recombinant XVII type collagen comprises a sequence shown in any one of SEQ ID NO.1-SEQ ID NO.3. The recombinant XVII type collagen can be highly expressed in an escherichia coli and pichia pastoris system, the expression system is simple, the cost is low, and the recombinant XVII type collagen is suitable for industrial production. The yield is high; the biological activity is good. The protein can be compounded with other proteins to form raw materials of tissue engineering products, cosmetics, health care products or medicines, so that the protein can be widely applied to the fields of medicines, medical instruments, biological materials, tissue engineering, cosmetics and the like.

The invention discloses an intelligent gradient extraction process and method for nutritional ingredients in yak bone marrow, and belongs to the technical field of bioactive substance extraction. The extraction method comprises the following four steps: gradient pressure supercritical degreasing, double-enzyme synergistic gradient enzymolysis, acid concentration gradient demineralization and temperature gradient gelatin extraction, and through the process coupling design of gradient pressure degreasing, buffer enzymolysis, graded acidolysis and membrane separation of gelatin, the high yield of the product in the previous stage is ensured; active structures of follow-up components are reserved to the greatest extent. Meanwhile, a sensing-decision-execution closed-loop system is constructed, real-time data sources such as NIR moisture sensing, online OPA detection and XRD in-situ analysis are integrated, technological parameters are dynamically adjusted through a multi-objective optimization algorithm, and global optimization of the yield, the purity and the energy consumption is achieved.

A pathogen surrogate, formed by a DNA tag or bar code and a carrier, is described for use in the validation and verification of sanitation, such as in food processing operations and for wash water systems for fresh produce. The carrier material is selected so that the pathogen surrogate mimics the behavior of a pathogen when subjected to a sanitation operation. One or more surrogates can be introduced in to an environment, which is then subjected to sanitation process, followed by a detection process using the DNA tag of the surrogate.

The invention provides recombinant IV type collagen and application thereof, and relates to the technical field of protein engineering. In the invention, an amino acid residue repetitive unit with good biological activity and stability in the human-derived IV-type collagen is found, and the amino acid residue repetitive unit is used as a core for repeating and constructing the recombinant IV-type collagen, so that the novel human-derived recombinant IV-type collagen with biological activity is obtained. The human-derived recombinant IV-type collagen provided by the invention is a small-molecular-weight protein, is easy to absorb by a human body, is good in safety, can remarkably promote secretion of collagen, also has the effects of promoting cell adhesion and cell migration, and has a good application prospect in the aspects of basement membrane repair and remodeling. A new functional component is provided for products for repairing and tightening the skin, resisting aging, resisting wrinkles, preserving moisture and the like.

The invention discloses recombinant IV-type collagen as well as a preparation method and application thereof, and belongs to the technical field of bioengineering. The amino acid sequence of the recombinant IV type collagen comprises a plurality of repetitive units, and the repetitive units are shown as SEQ ID NO. 1. The recombinant IV type collagen fragment is derived from human IV type collagen, heterologous amino acid residues are not introduced, and rejection and sensitization risks are avoided; meanwhile, the hydrogel also has good biological activity, including cell proliferation promoting activity and cell adhesion promoting activity, and is good in biocompatibility. In addition, the preparation method of the recombinant IV-type collagen is simple and easy to operate, and the recombinant IV-type collagen with high purity and stability can be obtained through the fermentation and purification method. Therefore, the recombinant IV type collagen disclosed by the invention has a relatively good application prospect.

The invention relates to a recombinant I-type humanized collagen with crosslinking property as well as a preparation method and application thereof, and belongs to the technical field of recombinant proteins. The invention relates to recombinant I-type humanized collagen with crosslinking property. The amino acid sequence of the recombinant I-type humanized collagen comprises an amino acid sequence as shown in SEQ ID No.1 or a derivative amino acid sequence with the sequence identity of more than 90% with the sequence as shown in SEQ ID No.1; the recombinant I-type humanized collagen has a triple helix structure. A complete triple helix structure can be efficiently expressed, and the hydrogel has efficient cross-linking capability, so that the hydrogel can be efficiently and stably formed through cross-linking.

The invention relates to the technical field of gene engineering, in particular to Escherichia coli for efficient soluble expression of recombinant human collagen III and construction and application thereof. The invention constructs Escherichia coli for efficient soluble expression of recombinant human III type collagen, and the Escherichia coli can co-express the recombinant human III type collagen and molecular chaperone which are regulated and expressed by signal peptide. Experiments prove that the engineering bacterium provided by the invention has the capability of efficient soluble expression of the recombinant human III-type collagen, and the recombinant human III-type collagen provided by the invention has good stability and anti-inflammatory effect.

The invention belongs to the technical field of biological medicine, and particularly relates to recombinant human XVII micromolecular collagen as well as a preparation method and application thereof. According to the invention, a recombinant human XVII type micromolecular collagen (Re-Hcol17) is constructed, and a stable triple helix structure is formed by connecting the 15th collagen domain, the 12th collagen domain, the 5th collagen domain and the 1st collagen domain in series. Experimental results prove that the Re-Hcol17 can significantly promote NIH / 3T3 fibroblast proliferation within the concentration range of 10-100 [mu] g / mL, the effect is better than that of natural human collagen, and extracellular matrix adhesion can be effectively promoted. Through genetic engineering and fermentation process innovation, the bottleneck that the human-derived XVII type collagen is difficult to efficiently express and unstable in structure is broken through, and a foundation is laid for wide application of the human-derived XVII type collagen in the fields of biological medicines and cosmetics.

The present invention relates to the technical field of protein engineering and provides a recombinant humanized type III collagen having a triple helix structure, a preparation method therefor, and a use thereof. The amino acid sequence of the recombinant humanized type III collagen comprises n core units, wherein n is 1 or an integer greater than 1, and the amino acid sequence of the core unit is as shown in SEQ ID NO: 1. The present invention further provides a method for constructing an expression system and a method for preparing a recombinant humanized type III collagen. The present invention further provides an actual industrial use on the basis of the characteristics of the protein. The recombinant humanized type III collagen provided by the present invention has high purity, good stability, and high biological activity. Experiments have shown that the recombinant humanized type III collagen has various biological activities such as promoting cell proliferation and migration.

The invention discloses a preparation method of micromolecular active collagen peptide, which comprises the following steps: (1) cutting fresh leather into fragments, pretreating the leather with a sodium bicarbonate solution, rinsing the leather with deionized water, and refrigerating and storing; (2) mixing papain, bromelain, pancreatin, pepsase, alkaline protease, neutral protease and flavourzyme to obtain a compound enzyme preparation; (3) performing high-pressure steam sterilization on the leather at 110-140 kPa and 120-122 DEG C to obtain leather with the hydrolysis degree of 75-85%, then adding distilled water into the leather to obtain mucilage, then adding a compound enzyme preparation into the mucilage, reacting for 5.5-6.5 hours at the pH of 6.8-7.2 and the temperature of 50-55 DEG C, and then performing enzyme inactivation at the temperature of 85-95 DEG C; and (4) after the reaction system is cooled to room temperature, purifying and centrifuging the reaction system, and taking clarified supernate, thereby obtaining the product. Different animal skins are treated, the proportion of peptide fragments with the molecular weight smaller than 1000 Da of the prepared small-molecule active collagen peptide is larger than or equal to 80%, and the hydroxyproline content is larger than 3%.

The invention relates to the technical field of collagen extraction, and provides a collagen extraction process for increasing hydroxyproline content, which sequentially comprises the steps of raw material pretreatment, deliming and degreasing, directional enzymolysis, gradient pressure-temperature synergistic extraction, purification, concentration and drying, a composite pretreatment agent containing a proline hydroxylase activator, EDTA-2Na and neutral protease is adopted in the raw material pretreatment; deashing and degreasing are combined with a chelating agent solution and ultrasonic treatment; a compound enzyme solution composed of trypsin, papain and proline hydroxylase is used for directional enzymolysis; a two-stage gradient pressure-temperature cooperation mode is adopted for extraction; purification is realized through combination of gel filtration chromatography and ion exchange chromatography; and finally carrying out freeze concentration and vacuum freeze drying to obtain the product. According to the process, through a multi-step synergistic effect, the content of hydroxyproline in collagen is remarkably increased, the product purity is high, natural functional characteristics are reserved, and the process is suitable for the fields of food, cosmetics, biological medicine and the like.

The invention provides a fish collagen peptide with a whitening effect and a preparation method thereof, and the method comprises the following steps: performing glycosylation modification treatment on fish collagen by using glucose, and then sequentially treating the fish collagen with gastric juice and intestinal juice to obtain the fish collagen peptide with a polypeptide sequence with glycosylation sites on a peptide chain. According to the invention, the fish collagen peptide with a remarkable inhibition effect on tyrosinase is obtained.

The invention relates to a recombinant elastin and a preparation method thereof as well as a recombinant elastin raw material and application thereof, and belongs to the technical field of recombinant proteins. The amino acid sequence of the recombinant elastin is an amino acid sequence as shown in SEQ ID No.1 or a derivative amino acid sequence of which the sequence identity with the SEQ ID No.1 is more than 90%. The protein is high in expression level, high in purity and relatively high in biological activity, and has the effects of supplementing skin collagen, resisting aging and repairing skin barriers.

Provided are a preparation method for a yeast-expressed type I recombinant human collagen with a tri-helical structure and use thereof. The preparation method comprises the steps of performing fermentation using an engineered bacterium and performing purification to obtain the type I recombinant human collagen with a tri-helical structure. A method for constructing the engineered bacterium comprises the step of transforming a host bacterium with plasmids pMChZ-α1(I), pMCrN-α2(I), pPIC9K-P4H(DP)-1, and pMCeH-[α1(I)] 2α2(I) to construct the engineered bacterium. The type I recombinant human collagen with a tri-helical structure prepared using the preparation method comprises hydroxyproline, and hydroxyproline accounts for 30% or more of total proline.

Method for generating a porous injectable scaffold that includes providing a liquid composition of 2 phases at a temperature below 25° C., of Newtonian behavior, where the composition comprises:a liquid dispersant phase at room temperature formed by a gelatin with a low melting point, less than 15° C., functionalized with methacryloyl or methacrylamide groups; and a photoinitiator;and a dispersed phase, of microdroplets or beads in solid state, of a gelatin solution with a melting point greater than 25° C.;initiating the polymerization of the dispersing phase by light radiation; raising the temperature to 35-40° C. and allowing melting of the dispersed phase; and obtaining a porous scaffold.The formed porous scaffold and its use as a biological support for tissue regeneration / generation; as a biological matrix as a support for cells, for cell invasion; as an acellular biological matrix, a biological matrix as a mechanical support and / or a biological matrix for active components.

Disclosed is a composition for treating dystrophic epidermolysis bullosa, the composition containing, among other things, a composition which includes cells that are derived from the lesions of dystrophic epidermolysis bullosa patients and that have been genetically engineered such as to produce type VII collagen.

The invention relates to the technical field of bioengineering, in particular to recombinant XVII type collagen with oxidation and aging resistance and an expression method and application thereof, the amino acid sequence of the collagen comprises n amino acid residue repetitive units, the sequence of the repetitive units is shown as SEQ ID NO.1, and n is larger than 1 and smaller than or equal to 60. The recombinant XVII type collagen provided by the invention has antioxidant and anti-aging activity, and is large in molecule quantity and easy to prepare.

The invention belongs to the technical direction of protein engineering in the technical field of biology, and particularly relates to a triple-helix folding and stabilizing method for recombinant collagen, which is a technology for efficiently assisting correct folding of human recombinant collagen expressed by escherichia coli and forming a stable triple-helix structure. The technology mainly solves the common key technical problems of low folding efficiency, unstable triple helix structure and the like of the recombinant collagen in an escherichia coli expression system, and obviously improves the yield of the functional recombinant collagen. The method has important application value in the fields of biomedical materials, tissue engineering, beauty and skin care and the like, and an efficient and economical technical path is provided for industrial production of recombinant collagen.

The invention provides a medical-grade recombinant three-type collagen and application thereof. The recombinant humanized three-type collagen has certain cell proliferation promoting capacity and is free of cytotoxicity. The medical-grade recombinant three-type collagen provided by the invention not only has the capability of promoting cell proliferation, is free of cytotoxicity and high in cell adhesion activity, but also has a three-helix structure characterized by the collagen and is extremely high in stability, the purity can reach about 85% after the collagen is induced for 120H in a 100L fermentation tank, the difficulty of a downstream purification process is greatly reduced, and the production cost is reduced. The effect in the aspect of cell activity is obvious.

The invention provides a preparation method of a terminal-peptide-free bovine type I collagen product. The preparation method comprises the following steps: obtaining a crushed bovine tissue raw material without impurities; the preparation method comprises the following steps: soaking a cattle tissue raw material in acid, and homogenizing to obtain cattle tissue homogenate; protease is added into the bovine tissue homogenate in batches for enzymolysis, the enzymolysis temperature is controlled to be 2-6 DEG C, after salting-out precipitation, pH value adjustment and redissolution are carried out on the bovine type I collagen extracting solution obtained in the middle batch, protease is added again for enzymolysis, salting-out precipitation, pH value adjustment and redissolution are carried out again, and the bovine type I collagen extracting solution is obtained. Repeating for multiple times to obtain a terminal-peptide-free bovine type I collagen solution; adjusting the pH value of the terminal-peptide-free bovine type I collagen solution, salting out, precipitating, centrifuging and washing to obtain terminal-peptide-free bovine type I collagen precipitate; and purifying the terminal-peptide-free bovine type I collagen precipitate to obtain the terminal-peptide-free bovine type I collagen product. According to the telopeptide-free bovine type I collagen product provided by the invention, no residual telopeptide is detected, and the purity is high.

The present invention is in the fields of medicinal chemistry, biotechnology and pharmaceuticals. The invention provides compositions comprising one or more collagen mimetic peptides, optionally attached to one or more therapeutic compounds or one or more imaging compounds, for use in methods of treating, preventing, ameliorating, curing and diagnosing certain diseases and physical disorders in humans and veterinary animals, as well as methods of manufacturing such composition. The invention also provides medical devices comprising one or more such compositions of the invention. The invention also provides methods of use of such compositions and devices in treating and diagnosing certain diseases and physical disorders in humans and veterinary animals, including ocular diseases or disorders, skin diseases or disorders, certain cancers, particularly intraluminal cancers, gastrointestinal diseases or disorders, genitourinary tract diseases or disorders, fibrotic diseases / disorders and rheumatic diseases / disorders.

The invention discloses a composite plant polypeptide composition with the effects of repairing pancreas and reducing blood sugar. The traditional Chinese medicine composition is prepared from the following raw materials in parts by weight: 10 to 50 parts of ginsenoside, 5 to 30 parts of radix astragali seu hedysari extract, 3 to 20 parts of radix rehmanniae polysaccharide, 2 to 15 parts of radix trichosanthis alkaloid, 5 to 25 parts of rhizoma dioscoreae polysaccharide, 5 to 30 parts of bitter gourd polypeptide, 3 to 20 parts of folium mori alkaloid, 8 to 40 parts of rhizoma polygonati polysaccharide, 5 to 25 parts of fructus hippophae flavone, 10 to 35 parts of wheat germ peptide, 2 to 15 parts of coptis berberine, 10 to 45 parts of corn stigma polysaccharide and 3 to 20 parts of saussurea involucrata polyphenol. 1-10 parts of sophora flavescens total alkaloids, 5-25 parts of a dendrobium extract, 5-30 parts of a radix puerariae extract, 8-35 parts of L-arabinose and 10-40 parts of small molecule peptides; 20 to 100 parts of collagen peptide and 15 to 80 parts of albumin peptide; 5-50 parts of microcrystalline cellulose, 3-30 parts of fructo-oligosaccharide and 0.5-5 parts of magnesium stearate; the limitation of single sugar control or simple component mixing in the prior art is broken through, a synergistic system of plant active components and functional polypeptides is constructed, and the purity and retention rate of the plant active components are improved by optimizing the extraction process.

There is provided a method of diagnosis comprising providing a sample previously isolated from a subject and analysing the sample for presence of a peptide comprising the amino acid sequence N- terminal-KSSTG (SEQ ID NO 1). The diagnosis may be for example diagnosis of a disease is selected from: osteoarthritis, early stage osteoarthritis, moderate osteoarthritis, osteoarthritis associated with risk for chip fractures of the joint or risk for avulsion fractures, severe osteoarthritis, microfractures of the joints, avulsion fractures and chip fractures of the joint.

The invention provides recombinant III-type collagen and application thereof, and relates to the technical field of genetic engineering. According to the invention, the yield of the collagen is improved by optimizing the nucleotide sequence of the target gene and optimizing the culture conditions of pichia pastoris, so that the collagen is efficiently expressed in engineering bacteria. The recombinant engineering bacterium shows strong potential in the aspect of improving the yield of protein with high economic value, and is suitable for large-scale industrial production. The recombinant III-type collagen is high in expression quantity, simple in preparation process and suitable for preparation of biological materials for medical cosmetology, wound repair and the like, and has a wide application prospect.

Provided herein are peptide amphiphiles (PAs) comprising a bioactive peptide, nanofibers displaying the bioactive PAs, and methods of use thereof. The disclosed peptide amphiphiles comprise a hydrophobic tail, a structural peptide segment, a charged peptide segment, and a bioactive IKVAV peptide. The disclosed PAs may be used in cell culture methods and in methods of treating central nervous system injury.

The present disclosure relates to compositions comprising collagen and hyaluronic acid, wherein the collagen is fully miscible with the hyaluronic acid. The present disclosure also relates to a composition comprising collagen, hyaluronic acid, and additional polymers, wherein the collagen is fully miscible with the hyaluronic acid and polymers. Methods of using the compositions described herein for medical and cosmetic treatments are also provided.

The invention provides a preparation method of human collagen and an application of the human collagen in anti-aging. The amino acid sequence of the human collagen is as shown in SEQ ID NO: 1; based on a natural collagen structure, a fusion sequence structure is provided, and the proportion of individual amino acids is adjusted; the collagen can promote skin cell growth and hyaluronic acid secretion; skin aging caused by ultraviolet radiation is resisted, inflammatory factor expression is inhibited, and oxidative stress is resisted.