Structural Collagen

Structural proteines — or fiber proteins — such as keratin, collagen, elastin, and silk have unique properties for bio-medical applications. Such proteins cannot yet be replaced with synthetic polymers. The main problem with such structural proteins is that their extraction from natural sources destroys their macro-scale structure. Thus, methods are needed of subsequently rebuilding structural proteins into the required shapes and sizes without losing their unique properties.

Hydrogen Link has has developed a method for macro–scale fibrillogenesis of structural proteins from their naturally derived building blocks. A method of instant self-assembling of protein fibrils can be used  for such proteins as gelatin, keratin or silk.

Gelatin (which is a denatured collagen in the form of a powder) is transformed into macro–scale fibrils of collagen, which can be shaped into various forms: thin membranes, tendon-resembling strips or hard and rigid pieces. A range of properties can be achieved, from dry and hard to soft and flexible. Alternatively, small scale micro-fibrils or collagen scaffolds can be formed.

Gelatin-derived "tendon" exhibits its internal collagen helix structure after elongation

Collagen fibrils or membranes are particularly suitable for use in wound healing or in plastic or reconstructive surgery. Our technique results in artificially shaped collagen with bio-mechanical and biological properties similar to those of native collagen, while containing no toxic or bio-incompatible agents.


Please contact us with inquires related to  our catalyst and materials at contact@hydrogenlink.com


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