flexible crosslinking technology

crosslinking

Crosslinking of collagen-based soft tissue scaffolds inhibits premature denaturing by high levels of matrix metalloproteinase (MMPs) that are present in higher levels in damaged or injured tissues.(1) Collagen scaffolds unable to resist digestion by these enzymes may not provide the appropriate structure to support organized host tissue remodeling.

Methods of crosslinking collagen-based biomaterials have previously involved the creation of rigid molecular bonds between collagen molecules. These crosslinks have traditionally been generated by exposure to harsh chemical agents such as glutaraldehyde or diisocyinates. Residual elements of this process have been identified to cause unwanted host tissue responses such as inflammation, calcification, and encapsulation. (2,3,4)

flexible crosslinking technology

Synovis Orthopedic and Woundcare’s crosslinking technology has advanced traditional methods of crosslinking by using a proprietary carbodiimide based process which introduces flexible bonds between the collagen molecules versus rigid zero length crosslinks.

EDC [1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride] based crosslinking has emerged in biomaterials research based on biocompatibility and non-cytotoxic residuals. Synovis Orthopedic and Woundcare has optimized this technology resulting in the development of biocompatible, stabilized, enzyme resistant collagen scaffolds to support host tissue remodeling.