141 results about "Collagen type" patented technology

The present invention relates to the field of biomedical materials, particularly to a novel composite collagen material for wound repair, and more specifically to a method for preparing a novel composite collagen material comprising recombinant humanized collagen type 21 (ColpepA1 21) and its use in wound repair. The present invention utilizes ColpepA1 21 to significantly promote key biological reactions in the wound healing process, including accelerating cell migration, enhancing skin hydration and barrier function, and improving the stability and elasticity of skin structure. The resulting novel composite collagen material effectively promotes wound healing and cell regeneration, alleviating oxidative damage.

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 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 provides a recombinant III-type humanized collagen gel based on a macromolecular crowding effect as well as a preparation method and application of the recombinant III-type humanized collagen gel. The method comprises the following steps: firstly, preparing an rhCol III solution system; then preparing a macromolecular crowding bath containing dextran 70, polyethylene glycol 8000 and ascorbic acid; then adding an rhCol III solution into the macromolecular crowding bath to form an rhCol III microgel; and finally, constructing a 3D printing molecular exclusion mold system which takes agarose as a substrate and contains a functional additive and a temperature-sensitive polymer as a temperature-sensitive release and spatial constraint component, so as to realize directional construction of the rhCol III microgel. According to the method disclosed by the invention, second-level physical gelling (lt; 15s) of rhCol is realized, and a physiological microenvironment supporting cell proliferation is constructed. The recombinant III-type humanized collagen gel prepared by the method can be used for preparing collagen microgel balls, collagen bundles, 3D (three-dimensional) bio-printing products and the like, and is wide in application range.

The present invention relates to the field of biomaterials, specifically a collagen material comprising recombinant humanized collagen type 21 (ColpepA1 21) and its application in facial augmentation. This invention utilizes collagen to not only provide an effective solution to skin aging but also promotes the natural synthesis of collagen within the skin, optimizing skin hydration and barrier function, and enhancing the skin's self-repair capacity. The resulting collagen material is a facial augmentation material. Through local injection or external application, it rapidly smoothes and firms the facial skin, while also improving overall skin health with long-term use.

The invention relates to the technical field of synthetic biology, in particular to polypeptide with a triple helix structure, recombinant XII type humanized collagen and application of the recombinant XII type humanized collagen. The recombinant XII type humanized collagen is successfully expressed and prepared, has a triple-helix structure and good biological activity including promotion of cell proliferation activity, cell adhesion activity and inhibition of MMP-1, is used as a biological material derived from a human body, does not generate immunological rejection and anaphylactic reaction when applied to the human body, and has a good application prospect. The composition can be used for medical or non-medical application of a plurality of tissues and organs of a human body, filling, compatibilizing or repairing, and promotion of skin compactness or wrinkle resistance and other scenes.

A method for preparing nondenatured collagen type II for alleviating joint pain includes pulverizing a cartilage raw material and defatting to obtain a total protein crude extract; adding anhydrous ethanol to the total protein crude extract, soaking, stirring, and centrifuging to obtain an anhydrous ethanol insoluble material; dissolving the anhydrous ethanol insoluble material in water, adjusting pH to acidic, stirring and centrifuging to obtain an acid-insoluble material; dissolving the acid-insoluble material in water, performing enzymatic hydrolysis and centrifuging to obtain an enzymatic hydrolysis precipitate; dissolving the enzymatic hydrolysis precipitate in water, followed by performing co-fermentation, and centrifuging to obtain a fermentation precipitate; and adding a water activity regulator to the fermentation precipitate, and then drying to obtain the nondenatured collagen type II. The content of protein, hydroxyproline and nondenatured collagen type II in the prepared nondenatured collagen type II is high, and the shelf life is prolonged.

The invention described herein relates to novel, non-naturally occurring, elastic, animal-component-free recombinant fusion biopolymers produced in plants by transient expression. More specifically, the present invention describes polynucleotides encoding fusion proteins of non-human sclerostin and human collagen wherein the fusion proteins are capable of forming hydroxylated triple helix fibers. The fusion protein is especially a fusion protein of spider silk protein-like protein and human collagen. More particularly, the present invention relates to a spider silk protein I / I type collagen fusion protein capable of forming a hydroxylated triple helix fiber, or a silk fibroin III / I type collagen fusion protein capable of forming a hydroxylated triple helix fiber. The present invention has improved properties (e.g., thermal stability, Young's modulus, cell adhesion, degradability, etc.) compared to native type I collagen. The invention also describes a method of use thereof, such as as defined in the claims for use as an electrospun scaffold particularly suitable for biomedical or cosmetic applications.

The invention relates to the technical field of recombinant proteins, and relates to a recombinant XII type collagen as well as a preparation method and application thereof. The recombinant XII type collagen is formed by connecting 5-30 repetitive units in series, and the amino acid sequence of each repetitive unit is as shown in SEQ ID NO: 1. The nucleic acid molecule is used for coding the recombinant XII type collagen; a vector comprises the nucleic acid molecule. According to the invention, a nucleotide sequence for coding the amino acid sequence is inserted into a vector to obtain a recombinant plasmid vector, then the recombinant plasmid vector is introduced into a host cell for culture, and then separation and purification are carried out to obtain the recombinant XII type collagen. The recombinant XII type collagen provided by the invention is easy to obtain, can realize efficient secretory expression, and meets the requirements of industrial production; the biological activity is good, and the proliferation and migration of human immortalized cartilage cells can be promoted.

The invention relates to the technical field of biology, and particularly discloses polypeptide, recombinant XIX type humanized collagen and application of the recombinant XIX type humanized collagen. The amino acid sequence of the polypeptide comprises n repetitive units; the repetitive unit comprises any one of the following amino acid sequences or variant sequences thereof: (1) an amino acid sequence as shown in any one of SEQ ID NO.1-2; (2) an amino acid sequence having at least 50%, 60%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98% or 99% sequence identity with the amino acid sequence as shown in any one of SEQ ID NO.1-2; (3) a variant sequence obtained by performing mutation of one or more amino acid residues on the amino acid sequence as shown in any one of SEQ ID NO.1-2; wherein n is an integer greater than or equal to 1. The polypeptide provided by the invention has a collagen triple helix structure, has good cell adhesion activity, can carry out functions of human collagen, is free of immunological rejection and anaphylactic reaction, and can be used in various fields of cartilage repair, biological dressing, tissue filling and the like.

The invention relates to the technical field of spectrum detection, in particular to a collagen detection method and device. The method comprises the following steps: acquiring an infrared spectrogram of collagen to be detected; screening out target absorption peaks generated without noise based on the distribution condition of the absorption peaks in the infrared spectrogram; according to the position of the wave band corresponding to the target absorption peak, obtaining a collagen type corresponding to each target absorption peak; obtaining the content of each collagen type according to the areas of all the target absorption peaks corresponding to each collagen type; and determining the function of the collagen to be detected based on the content of each collagen type. According to the method, the collagen type corresponding to the target absorption peak is accurately determined, so that the condition of collagen type confusion is avoided, the content of each collagen type is accurately obtained, and the function of the to-be-detected collagen is accurately analyzed.

The present disclosure relates to amino acid and plant extract compositions and uses thereof, and also to joint care compositions comprising the amino acid and plant extract. The composition disclosed by the invention can increase bone hardness, prevent inflammatory response, relieve arthralgia and / or improve joint flexibility, so that systematic support is provided for bone and joint health.

The invention discloses a recombinant II-type collagen with a cartilage filling effect and application of the recombinant II-type collagen. The amino acid sequence of the recombinant II type collagen is as shown in SEQ ID NO: 1. By intercepting amino acids from the 722nd site to the 955th site of the natural II-type collagen, the recombinant II-type collagen which is easy to produce and has a cartilage filling effect superior to that of the full-length II-type collagen can be obtained.

The present application provides gastrodia elata (Blume) alkaloids PFT201A, PFT201B and PFT203 and a preparation method thereof, and application thereof in the fields of cosmetics and medicine. Gastrodia elata Gastrodia elata (Blume) alkaloids PFT201A, PFT201B and PFT203 significantly promote the secretion of collagen type II in human dermal fibroblasts-adult (HDFa) at an extremely low concentration (0.1 μ M), and have no cytotoxicity at the concentration. These compounds can be used for preparing anti-aging drugs or skin care products.

This patent application discloses a recombinant human type II collagen, its preparation method, and its uses. The recombinant human type II collagen of this patent application is a truncated protein of natural human type II collagen, and its amino acid sequence is shown in SEQ ID No: 1. The recombinant human type II collagen of this invention can be expressed in commercial expression systems such as the commercial Pichia pastoris expression system with high expression yields. Furthermore, its tested biological activities (promoting cell proliferation and wound healing) are significantly superior to those of natural human type II collagen, and also significantly superior to other stages of natural human type II collagen.

The invention relates to the technical field of biological agents, and provides a recombinant III-type collagen / platycladus orientalis essential oil nanoemulsion which is prepared from the following raw materials in percentage by weight: 15-35% of recombinant III-type collagen, 1-10% of platycladus orientalis essential oil and the balance of pure water. The invention also provides a preparation method of the nanoemulsion, which comprises the following steps: weighing the recombinant III collagen and the pure water according to the weight percentage, mixing and dissolving, then adding the platycladus orientalis essential oil, stirring and uniformly mixing to form primary emulsion, and carrying out high-speed shearing for 3-9 minutes by using a high-speed shearing emulsifying machine at the rotating speed of 8000r / min, so as to obtain the recombinant III collagen nanoemulsion. The recombinant III type collagen / platycladus orientalis essential oil nanoemulsion is obtained. The prepared oriental arborvitae essential oil nanoemulsion is uniform in size, high in stability and easy to store. The recombinant III type collagen has good biological activity and degradability, and can effectively reduce the irritation. The prepared nanoemulsion can significantly improve the antibacterial property of the platycladus orientalis essential oil nanoemulsion, and has a good prospect in application to bacterial infectious wounds.

The application discloses a kind of benzofused heterocyclic ring amine pyrazolopyrimidine ketone derivatives, preparation method and application, belong to the technical field of pharmaceutical chemistry, the compound of the application has the structure shown in formula (I) or its pharmaceutically acceptable salt.The preparation method is with amino pyrazole as starting material, cyclization, chlorination, selective hydrolysis is prepared pyrazolopyrimidine ketone nucleus, again, the target compound is obtained by nucleophilic substitution reaction with benzofused heterocyclic ring substituted cyclic amine side chain of nucleus, simple operation, suitable for industrial production.The in vitro activity evaluation result shows that compound can significantly inhibit TGF-β1 induced hepatic stellate cell activation, effectively down-regulate the expression of fibronectin and collagen type I;Animal in vivo pharmacodynamics experiment further confirms that representative compound can dose-dependently reduce the degree of CCl4 induced mouse liver fibrosis, reduce collagen deposition, improve liver tissue pathological damage after oral administration (I).

This invention provides the application of type IV collagen and its encoding gene in the prognostic assessment and treatment of nasopharyngeal carcinoma (NPC). Research has shown that high expression of type IV collagen and its encoding gene COL4A1 is significantly associated with lower T-cell infiltration in patients with recurrent NPC; compared to NPC patients with low expression of type IV collagen, those with high expression have worse LRRFS and OS; and the expression level of the type IV collagen encoding gene COL4A1 is significantly associated with worse PFS in NPC patients. Therefore, type IV collagen and its encoding gene COL4A1 can serve as specific prognostic biomarkers for assessing the prognosis of NPC patients. Furthermore, inhibiting the expression of type IV collagen can effectively inhibit the growth of NPC; therefore, agents that inhibit type IV collagen expression can be used as drugs to inhibit immune escape in NPC and for the treatment of NPC.

The present invention discloses the use of Avn Anthramides C (Avn C) as an inducer of chondrocytic differentiation in Mesenchymal Stem Cells (MSCs), providing a promising approach for regenerative cartilage therapy. By employing Avn C treatment, MSCs exhibit enhanced chondrocytic differentiation and elevated expression of key specific chondrogenic extracellular matrix (ECM) factors, notably Collagen Type II (COL2A1). Furthermore, when Avn C is used in combination with Chondroitin Sulfate (CS), a synergistic effect is observed, leading to upregulation of the transcriptional activity state of SOX9, a key regulator of chondrogenesis. The disclosed invention shows significant improvements in mRNA gene expression (ACAN, LRP1, SOX9), cellular protein levels (COL2A1, SOX9, LRP1), and functional outcomes, as evidenced by the secretion of extracellular matrix proteins (FSTL-1, BGH3, CO1A1, CO1A2, and CO3A1).

The application discloses a kind of antibody for detecting collagen type IV alpha 3, detection kit and its application, belong to immunodetection technical field.Wherein, the antibody for detecting collagen type IV alpha 3 is COL4A3 monoclonal antibody, the COL4A3 monoclonal antibody can specifically recognize collagen type IV alpha 3, such as the protein fragment shown in SEQ ID NO:9.The application further discloses an antibody combination comprising the COL4A3 monoclonal antibody.The application further discloses the application of the COL4A3 monoclonal antibody or antibody combination in the preparation of collagen type IV detection kit and the kit prepared by the same.The kit of the application has very great clinical application value for detecting Alport syndrome with high specificity and strong sensitivity.

The application provides a composition containing curcuma and type II collagen-containing cartilage powder and application thereof in joint maintenance, and relates to the field of food technology. The application provides a composition containing milk mineral salt, curcuma, type II collagen-containing cartilage powder, enzymatic bone powder, N-acetyl glucosamine and black pepper extract, which can significantly repair joint damage, significantly reduce cartilage damage indexes such as CTX-II and COMP, and can be used for preparing a joint maintenance medicine.

This invention relates to the field of biotechnology, specifically disclosing a novel polypeptide, recombinant XIX type humanized collagen, and their applications. This invention provides a novel polypeptide with good cell adhesion activity and the ability to promote cell proliferation. The amino acid sequence of the polypeptide comprises n repeating units; each repeating unit comprises any one of the following (1)-(3) amino acid sequences or their variants: (1) the amino acid sequence shown in SEQ ID NO.1; (2) an amino acid sequence having at least 50%, 60%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99% sequence identity with the amino acid sequence shown in SEQ ID NO.1; (3) a variant sequence obtained by mutating one or more amino acid residues of the amino acid sequence shown in SEQ ID NO.1; wherein n ≥ 1 and is an integer. The polypeptide of this invention can be used in various fields such as promoting skin barrier repair, wound healing, and epidermal renewal.

The application provides a high-activity and high-expression recombinant collagen type XVII and application thereof, and belongs to the technical field of protein engineering, wherein the amino acid sequence of the recombinant collagen type XVII is formed by repeating and connecting n core units, wherein n is an integer of 1 or greater than 1, and the amino acid sequence of the core unit is shown as SEQ ID NO:1; the application further provides a construction method of various expression systems and a preparation method of the recombinant collagen type XVII; and the application further provides actual industrial applications according to the characteristics of the protein. The recombinant collagen type XVII provided by the application has high purity, high yield and high biological activity, and the molecular weight is much smaller than that of natural collagen protein, so that the collagen protein can reduce the barrier to biological function through the skin barrier, and experiments show that the collagen protein has multiple biological activities such as promoting cell migration.

A recombinant humanized collagen type I alpha-1 (rhCol1A1), and an expression vector and use thereof are provided, belonging to the technical field of bioengineering. The rhCol1A1 has an amino acid sequence of SEQ ID NO: 1. This aim is to solve the problem of difficulty in expressing soluble full-length humanized collagen in Escherichia coli prokaryotic expression systems, and differences between the recombinant collagen and humanized collagen in yeast expression systems. It is proposed that the rhCol1A1 chain is expressed in Expi293F™ human embryonic kidney cells, and the protein expression level is increased using a fusion expression plasmid, enabling the expression of full-length humanized collagen type I alpha 1 chain. Activity studies have shown that the expressed rhCol1A1 exhibits a desirable activity in promoting cell migration, and may be widely used in the fields of biomedicine, tissue engineering, skin care, and food.

The present application relates to the field of cosmetics, in particular to an endogenous antioxidant anti-wrinkle composition, a preparation method and application thereof, the composition comprises acetyl tetrapeptide-5, CycloRetin, collagen type 21, acetyl hexapeptide-8 and vitisins, the composition can promote the synthesis of collagen in the extracellular matrix of the dermis of the skin, and can improve the tightening and anti-wrinkle effect, human test proves that the tightening and anti-wrinkle effect of the composition is the best.

The invention discloses haliotis discus hannai I-type collagen peptide as well as a screening method and application thereof, and belongs to the technical field of bioactive peptides. The peptide sequences of the haliotis discus hannai I type collagen peptide are GAAGDK and DSQSAR; the screening method specifically comprises the following steps: (1) virtual enzymolysis of the haliotis discus hannai I-type collagen; (2) screening the bioactive peptide; and (3) molecular docking. According to the invention, through rational design and a virtual screening strategy, a human gastrointestinal tract digestion process is simulated to carry out targeted virtual enzymolysis, a multi-target molecular docking technology is combined, brand-new bifunctional peptides GAAGDK and DSQSAR are accurately predicted and screened from a specific collagen sequence, and aiming at a dual-action mechanism of AGE-RAGE axis and oxidative stress, the application has the advantages of high sensitivity, high sensitivity and high stability. The composition has remarkable synergistic interaction potential in the aspects of preventing diabetic complications and delaying skin and body senescence, and a brand new core raw material is provided for developing next-generation anti-saccharification functional food and skin care products.

The application relates to a recombinant type I collagen and application thereof, which utilizes the characteristics of Pichia pastoris capable of secreting and expressing recombinant proteins, secretes the recombinant type I collagen on the culture medium supernatant, and reduces the difficulty of protein purification. In addition, the integrin site RGD is inserted into the collagen to form a recombinant type I collagen with high stability and high expression. According to the relative proliferation of cells and the relative adhesion experiment of cells, it can be seen that the recombinant type I collagen has the effects of promoting the proliferation of skin fibroblasts, improving the skin, promoting wound healing, promoting the adhesion of fibroblasts in the skin layer and the like. Therefore, the recombinant type I collagen has great potential applications in the fields of skin care and beauty, medical treatment and the like.

The invention described herein relates to a novel non-naturally occurring, elastomeric animal-free recombinant fusion biopolymers produced in plants through transient expression. More specifically, the present invention describes polynucleotides encoding fusion proteins of a non-human scleroprotein with a human collagen, wherein said fusion protein is capable of forming hydroxylated triple helix fibers. In particular fusion proteins of a Spidroin like protein with a human collagen. More in particular, eithera Spidroin-I / Collagen Type-I fusion protein, capable of forming hydroxylated triple helix fibers, or a Fibroin-III / Collagen Type-I fusion protein, capable of forming hydroxylated triple helix fibers. The present invention has improved properties (e.g., thermostability, young's modulus, cell adhesion, degradability, and the like) versus that of native Collagen Type-I. Also described are methods for use thereof, such as the use of electrospun scaffolds which are particularly well suited for biomedical or cosmetic applications as defined in the claims.

The present disclosure provides a recombinant humanized collagen VIII, which is a triple helix structure, has good cell adhesion activity, and is applied to human body without immune rejection and allergic reaction.

To provide osteoblasts and compositions comprising the osteoblasts for treating bone diseases.SOLUTION: Disclosed is an osteoblast having both proliferation ability and differentiation ability, where the osteoblast has higher expression levels of connexin 43, RUNX2 and collagen type 1A compared with those of undifferentiated stem cells and mature osteocytes; higher expression levels of angiopoietin and alkaline phosphatase compared with those of undifferentiated stem cells; and lower expression levels of osterix, osteocalcin and osteopontin compared with those of mature osteocytes. Also, the osteoblast has a lower Ki-67 expression level compared with that of undifferentiated stem cells.SELECTED DRAWING: Figure 1