76 results about "Collagen fibril" patented technology

A method of using a substantially non-porous equine collagen foil to repair and regenerate dura mater tissue of mammals when the dura mater tissue is damaged as a result of injury, tumors, surgery, and the like. The non-porous equine collagen foil comprises collagen fibrils which provides a replacement dura mater composition that is elastic, liquid-tight, and which has a high tensile strength. The non-porous equine collagen foil is furthermore resorbable and provides a biomatrix, wherein a neodura is rapidly formed which becomes indistinguishable from the autologous dura mater in a matter of weeks. The process for making the equine collagen foil reduces the likelihood of disease transmission.

Bone matrix compositions having nanoscale textured surfaces and methods for their production are provided. In some embodiments, bone matrix is prepared for implantation and retains nanoscale textured surfaces. In other embodiments, nanostructures are imparted to bone matrix wherein collagen fibrils on the surface of the bone matrix have been compromised, thus imparting a nanoscale textured surface to the bone matrix. Generally, these methods may be applied to mineralized or demineralized bone including partially or surface demineralized bone.

Methods and devices for applying high intensity focused ultrasound to modulate collagen in animal tissue (such as to disrupt collagen fibrils in a mammal, such as a human), particularly to enhance the aesthetic appearance of skin, and / or to otherwise improve skin conditions.

A method of using a substantially non-porous equine collagen foil to repair and regenerate dura mater tissue of mammals when the dura mater tissue is damaged as a result of injury, tumors, surgery, and the like. The non-porous equine collagen foil comprises collagen fibrils which provides a replacement dura mater composition that is elastic, liquid-tight, and which has a high tensile strength. The non-porous equine collagen foil is furthermore resorbable and provides a biomatrix, wherein a neodura is rapidly formed which becomes indistinguishable from the autologous dura mater in a matter of weeks. The process for making the equine collagen foil reduces the likelihood of disease transmission.

A method of accurately fabricating a non-human donor corneal tissue for implantation into a recipient human cornea, the method comprising the steps of: removing corneal tissue from a donor with a femtosecond laser; placing the corneal tissue in a fixative solution for a selected time interval to cross-link the collagen fibrils in the tissue and prevent swelling of the corneal tissue; and shaping the tissue to provide a conical inlay of a selected shape and thickness having one or more radial extensions. The method is such that the corneal inlay may be attached to the peripheral corneal and / or the sclera. The method is such that the corneal inlay may be stored for a period of up to two years prior to attachment.

The present invention relates to a tissue-engineered intervertebral disc (IVD) suitable for total disc replacement in a mammal and methods of fabrication. The IVD comprises a nucleus pulposus structure comprising a first population of living cells that secrete a hydrophilic protein and an annulus fibrosis structure surrounding and in contact with the nucleus pulposus structure, the annulus fibrosis structure comprising a second population of living cells and type I collagen. The collagen fibrils in the annulus fibrosis structure are circumferentially aligned around the nucleus pulposus region due to cell-mediated contraction in the annulus fibrosis structure. Also disclosed are methods of fabricating tissue-engineered intervertebral discs.

The invention relates to engineered matrices comprising collagen fibrils with specific characteristics, including, but not limited to, a specific fibril area fraction (i.e., density) and / or a specific elastic or linear modulus (i.e., stiffness). The invention also relates to methods of preparation and use of the matrices.

Described herein is a method for producing a biofabricated material from collagen or collagen-like proteins which are recombinantly produced and which contain substantially no 3-hydroxyproline. The collagen or collagen-like proteins are isolated from animal sources, or produced by recombinant DNA techniques or by chemical synthesis. The collagen or collagen-like proteins are fibrillated, crosslinked, dehydrated and lubricated thus forming the biofabricated material having a substantially uniform network of collagen fibrils.

The invention is directed to a method for producing a composite material comprising a biofabricated material and a secondary component. The secondary component may be a porous material, such as a sheet of paper, cellulose, or fabric that has been coated or otherwise contacted with the biofabricated material. The biofabricated material comprises a uniform network of crosslinked collagen fibrils and provides strength, elasticity and an aesthetic appearance to the composite material.

Methods of stabilizing collagen fibrils in a cornea are disclosed. The stabilization may be effected by treating the cornea with a protein that crosslinks collagen fibrils, such as decorin. The stablization methods include treatment of corneas before, during, or after a surgical procedure, treatment of keratectasia, and treatment of keratoconus.

Methods of increasing the permeability of corneal epithelium to facilitate the diffusion of agents into the collagen fibrillar network of the stroma are provided. Used in combination, these methods open the epithelium to facilitate diffusion of stabilization molecules into the stroma and dissociate bridging molecules from stromal collagen fibers, thereby priming the collagen fibrillar network for restabilization by stabilization molecules. These methods can be used to increase the effectiveness and longevity of non-invasive corneal reshaping, such as orthokeratology, for correcting myopia, hyperopia and astigmatism.

A leather substrate formed from waste leather and its method of production, particularly a leather substrate made up substantially of a collagen fibril matrix.

Compositions and methods of preparing a graft construct comprising aligned collagen fibrils, wherein the construct is anisotropic, are described. The construct is prepared by application of an electrochemical field and a pH gradient to solutions containing collagen. In accordance with this method, collagen aligns at its isoelectric point to form anisotropic constructs.

A leather substrate formed from waste leather and its method of production, particularly a leather substrate made up substantially of a collagen fibril matrix.

Described herein is a method for producing a biofabricated material from collagen or collagen-like proteins. The collagen or collagen-like proteins are isolated from animal sources or produced by recombinant DNA techniques or by chemical synthesis. The collagen or collagen-like proteins are fibrillated, crosslinked, dehydrated and lubricated thus forming the biofabricated material having a substantially uniform network of collagen fibrils.

The invention is directed to a class of fiber or strand suspension compositions that may be processed further into viscoelastic pastes or porous solids. The preferred compositions of the invention comprise biologically derived or biologically compatible materials, such as collagen, that can be injected or implanted for tissue augmentation or repair. This invention is also directed to methods of making these compositions and to apparatus that can be used to make the compositions.

A biofabricated material containing a network of crosslinked collagen fibrils is disclosed. This material is composed of collagen which is also a major component of natural leather and is produced by a process of fibrillation of collagen molecules into fibrils, crosslinking the fibrils and lubricating the crosslinked fibrils. Unlike natural leathers, this biofabricated material exhibits non-anisotropic (not directionally dependent) physical properties, for example, a sheet of biofabricated material can have substantially the same elasticity or tensile strength when stretched or stressed in different directions. Unlike natural leather, it has a uniform texture that facilitates uniform uptake of dyes and coatings. Aesthetically, it produces a uniform and consistent grain for ease of manufacturability. It can have substantially identical grain, texture and other aesthetic properties on both sides distinct from natural leather where the grain increases from one side (e.g., distal surface) to the other (proximal inner layers).

A leather substrate formed from waste leather and its method of production, particularly a leather substrate made up substantially of a collagen fibril matrix.

A biofabricated material containing a network of crosslinked collagen fibrils is disclosed. This material is composed of collagen which is also a major component of natural leather and is produced by a process of fibrillation of collagen molecules into fibrils, crosslinking the fibrils and lubricating the crosslinked fibrils. Unlike natural leathers, this biofabricated material exhibits non-anisotropic (not directionally dependent) physical properties, for example, a sheet of biofabricated material can have substantially the same elasticity or tensile strength when stretched or stressed in different directions. Unlike natural leather, it has a uniform texture that facilitates uniform uptake of dyes and coatings. Aesthetically, it produces a uniform and consistent grain for ease of manufacturability. It can have substantially identical grain, texture and other aesthetic properties on both sides distinct from natural leather where the grain increases from one side (e.g., distal surface) to the other (proximal inner layers).

The invention is directed to a composite material comprising a biofabricated material and a secondary component. The secondary component may be a porous material, such as a sheet of paper, cellulose, or fabric that has been coated or otherwise contacted with the biofabricated material. The biofabricated material comprises a uniform network of crosslinked collagen fibrils and provides strength, elasticity and an aesthetic appearance to the composite material.

The present invention relates to scanning confocal microscopy used to systematically quantify characteristic collagen fibril orientations by position within the lamellar thickness of secondary osteons along the osteon radial direction. Fully calcified lamellar specimens appear either extinct or bright in cross-section under circularly polarized light, and can be isolated from embedded osteon, flattened, and examined along the radial thickness direction of the original embedded osteon. Collagen orientation is measured from confocal image stacks. Extinct and bright lamellae display distinct patterns of collagen orientation distribution. Relative counts of collagen fibrils that are longitudinal to the osteon axis in extinct lamellae, transverse to the osteon axis in bright lamellae, and oblique to the osteon axis in both lamellar types, show parabolic distribution through the osteon radial direction.

A biofabricated material containing a network of crosslinked collagen fibrils is disclosed. This material is composed of collagen which is also a major component of natural leather and is produced by a process of fibrillation of collagen molecules into fibrils, crosslinking the fibrils and lubricating the crosslinked fibrils. Unlike natural leathers, this biofabricated material exhibits non-anisotropic (not directionally dependent) physical properties, for example, a sheet of biofabricated material can have substantially the same elasticity or tensile strength when stretched or stressed in different directions. Unlike natural leather, it has a uniform texture that facilitates uniform uptake of dyes and coatings. Aesthetically, it produces a uniform and consistent grain for ease of manufacturability. It can have substantially identical grain, texture and other aesthetic properties on both sides distinct from natural leather where the grain increases from one side (e.g., distal surface) to the other (proximal inner layers).

Methods of stabilizing and organizing collagen fibrils in extracellular matrix of retinal tissues, particularly Bruch's membranes, and stabilizing retinal pigment epithelial layers lining Bruch's membrane are disclosed. The stabilization and organization may be effected by treating retinal tissues with a protein that crosslinks and organizes collagen fibrils, such as decorin. The stabilization and organization methods include treatment of retinal tissues before, during, or after diagnosis of dry macular degeneration, diagnosis of early stages of diabetic retinopathy and diabetic macular edema to prevent, retard, or limit progression of disorganization of Bruch's membrane and disorganization of retinal pigment epithelial cells lining Bruch's membrane.

The invention discloses collagen and an extraction method thereof. The method includes the steps: 1) refrigerating and rubbing animal tissues containing the collagen in liquid nitrogen; 2) extractingthe collagen from the rubbed animal tissues by an acid / enzyme method to obtain collagen solution; 3) dialyzing and freeze-drying the collagen solution to obtain the powdery collagen. By the refrigeration-rubbing pretreatment method, the animal tissues containing the collagen is refrigerated in the liquid nitrogen in advance for a period of time and rubbed into powder under a certain frequency by arubbing instrument, a triple-helical structure and thermal denaturation temperature cannot be affected after treatment by the method, compared with an original acid-extraction method without refrigeration-rubbing, the extraction rate of the method is increased by 18%-82%, and the method is of great significance for application of the collagen and collagen-based biological materials.

The invention relates to peptides including DEDE(SSD)nDEG indicated by SEQ NO. 1, RRRDEDE(SSD)nDEG indicated by SEQ No. 2, RRRGDEDE(SSD)nDEG indicated by SEQ No. 3, and LKKLKKLDEDE(SSD)nDEG indicated by SEQ NO. 4, wherein n is an integer from 2 to 20. The invention also relates to phosphorylating these peptides at multiple amino acid sites by employing casein kinases. These phosphorylated peptides may be used in various applications such as forming mineralized collagen fibrils and biomimetic composites for use in tissue repair and regeneration.

A method for restructuring a biological tissue comprising collagen fibrils selected from a venous tissue, a cardiac valvular tissue, a cutaneous or subcutaneous tissue, a tissue of a muscular tendon, a tissue of a muscular fascia or a tissue of a muscular aponeurosis, comprising the following operational steps: a) bringing into contact a biological tissue comprising collagen fibrils with a cross-linking chemical composition able to induce cross-linking of collagen fibrils consequent to activation through electromagnetic radiation; b) activating said cross linking chemical composition through exposure to an electromagnetic radiation; c) cross-linking the collagen fibrils of said biological tissue in order to obtain a restructured biological tissue. The method according to the invention can be applied to recover a venous continence and both a venous and a cardiac valve diameter. The method reduces the visibility of cutaneous wrinkles, reinforces or repairs tendons, muscular fascia and aponeurosis as well as to heals surgical or traumatic cutaneous wounds or cutaneous ulcers.

Methods of stabilizing collagen fibrils in a cornea are disclosed. The stabilization may be effected by treating the cornea with a protein that crosslinks collagen fibrils, such as decorin. The stablization methods include treatment of corneas before, during, or after a surgical procedure, treatment of keratectasia, and treatment of keratoconus.

Bone matrix compositions having nanoscale textured surfaces and methods for their production are provided. In some embodiments, bone matrix is prepared for implantation and retains nanoscale textured surfaces. In other embodiments, nanostructures are imparted to bone matrix wherein collagen fibrils on the surface of the bone matrix have been compromised, thus imparting a nanoscale textured surface to the bone matrix. Generally, these methods may be applied to mineralized or demineralized bone including partially or surface demineralized bone.

The invention provides bionic mineralized collagen gel and a preparation method and application thereof, and belongs to the technical field of bionic materials. Polyaspartic acid is adopted as a stabilizer, a mineralization solution containing calcium ions and phosphate ions can form amorphous calcium phosphate nano-clusters, after collagen hydrogel is mixed with the amorphous calcium phosphate nano-clusters, the amorphous calcium phosphate nano-clusters can enter collagen fibrils in the collagen hydrogel and be combined with free carboxyl, then nucleating and phase change are performed to form hydroxyapatite, the hydroxyapatite grows in order in the long axis direction of the collagen fibrils, and mineralization in the collagen fibrils in the collagen gel is achieved.

This invention relates to methods for preparing biomaterials by applying multiple cycles of tensile loading to compacted collagen gels in order to fuse the collagen fibrils together within the compacted gels. This produces a biomaterial with improved material properties. Biomaterials produced by such methods may be useful, for example, as tissue equivalent implants, in the repair and / or replacement of damaged tissue in an individual.