The invention relates to a wound dressing which is particularly suitable for therapeutically dressing wounds. Said wound dressing consists of a multi-layered structure comprising at least one layer containing at least one hydrocolloid, preferably collagen, (“hydrocolloid layer” or “collagen layer”) and at least one layer containing an activated carbon (“activated carbon layer”).

The present invention resides in a method for producing jellyfish collagen hydrogels and kits for producing the same. The jellyfish collagen hydrogels can be used in the culture of cells. According to the invention, there is a process for producing jellyfish collagen hydrogels comprising jellyfish collagen fibrils, said process comprising the steps of: mixing a solution of purified jellyfish collagen and an aqueous neutralisation buffer; and incubating the mixture for a sufficient time to enable jellyfish collagen fibrils to form, wherein a cross-linking agent is either added during to mixing step or during or after the incubation of the mixture.

The present disclosure provides synthetic collagen and methods of making and using synthetic collagen that include a synthetic collagen that facilitates wound closure comprising an isolated and purified triple helical backbone protein that facilitates wound closure comprising one or more alteration in a triple helical backbone protein sequence, that stabilize the isolated and purified triple helical backbone protein and does not disrupt an additional collagen ligand interaction; and one or more integrin binding motifs, wherein the isolated and purified triple helical backbone protein facilitates wound closure.

The application relates to a method and apparatus for manufacturing a natural fiber based staple fibers. The application further relates to the staple fibers, staple fiber based raw wool and products comprising such. A method comprises providing a cellulose suspension (101, 310, 510) including water, refined cellulose fibrils and at least one rheology modifier, directing the cellulose suspension through a nozzle (102, 320, 520) onto a surface (300, 400, 500), drying the cellulose suspension onto the surface (103, 300, 400, 500) for forming a fiber (350, 550), and cutting the cellulose suspension on the surface for forming staple fibers (105).

Disclosed is a hydrophilic dressing (200) having appropriate mechanical strength, comprising a composite material (100, 220) and a film (210). The composite material (100, 220) comprises a hydrophilic substrate material (110) and a compound (120) that promotes wound healing, wherein the hydrophilic substrate material (110) is a reaction product of a hydrophilic polymer, wherein the hydrophilic polymer comprises a hydrophilic monomer, a cross-linking agent and an inorganic silicon-oxygen compound, wherein the compound (120) that promotes wound healing is distributed in the hydrophilic substrate material (110).

Disclosed is a hydrophilic dressing (200) having appropriate mechanical strength, comprising a composite material (100, 220) and a film (210). The composite material (100, 220) comprises a hydrophilic substrate material (110) and a compound (120) that promotes wound healing, wherein the hydrophilic substrate material (110) is a reaction product of a hydrophilic polymer, wherein the hydrophilic polymer comprises a hydrophilic monomer, a cross-linking agent and an inorganic silicon-oxygen compound, wherein the compound (120) that promotes wound healing is distributed in the hydrophilic substrate material (110).

Haemostatic wound dressings are described. The dressings comprise a non-colloidal porous dressing material, and a plurality of fibrinogen-binding peptides immobilised to the non-colloidal porous dressing material, wherein each fibrinogen-binding peptide comprises: an amino acid sequence Gly-Pro-Arg-Xaa (SEQ ID NO: 1) at an amino-terminal end of the peptide, wherein Xaa is any amino acid other than Val, preferably Pro, Sar, or Leu; or an amino acid sequence Gly-His-Arg-Xaa (SEQ ID NO: 2) at an amino-terminal end of the peptide, wherein Xaa is any amino acid other than Pro. The dressings are able to accelerate haemostasis without requiring enzymatic activity. In particular, the dressings to do not rely on the action of exogenous thrombin, and can be stored long-term at room temperature in solution. Methods of making the dressings, and use of the dressings to control bleeding are also described.

A mechanism and a method for slitting silicone membranes using automated slitting blades is presented. The pattern of slits in the membrane can be adjusted by using a cutting cylinder comprised of a plurality of circular cutting gears assembled in parallel.

The cutting cylinder is of indefinite length, but in the preferred embodiment is approximately 15″ long and 3″ in diameter. The silicone membrane can range in thickness from 0.005″ to 0.01″ inch.

The present invention provides polypeptides comprising or consisting of an amino acid sequence derived from collagen type VI or a fragment, variant, fusion or derivative thereof, or a fusion of said fragment, variant of derivative thereof, wherein the polypeptide, fragment, variant, fusion or derivative is capable of killing or attenuating the growth of microorganisms. Related aspects of the invention provide corresponding isolated nucleic acid molecules, vectors and host cells for making the same. Additionally provided are pharmaceutical compositions comprising a polypeptide of the invention, as well as methods of use of the same in the treatment and/or prevention of microbial infections and in wound care. Also provided are a method of killing microorganisms in vitro and a medical device associated with the pharmaceutical composition.

The technology described in this application provides a dressing (as well as uses, systems, and methods including such dressing) that includes a contact layer with a first surface configured to contact a tissue site in a subject and includes a scaffold configured to structurally support the contact layer, where the contact layer includes a bioresorbable material. The dressing may advantageously exhibit protease-modulating activity under physiological conditions.