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Thrombin-free polymerization leads to pure fibrin(ogen) materials with extended processing capacity

Abstract : Fibrin is a key protein for various clinical applications such as tissue reconstruction. However, in contrast to type I collagen, fibrin shaping has so far faced major limitations related to the necessity to add thrombin enzyme to fibrinogen precursors to induce fibrin self-assembly. Here we report a thrombin-free gelation pathway of fibrinogen solutions by incubation at 37°C in mild acidic conditions. We unravel the biochemical mechanisms underlying the gelation process and draw comparison between fibrinogen and fibrin at both molecular and supramolecular levels in these conditions. The protocol enables to control the viscosity of fibrin(ogen) solutions, and to induce fibrin(ogen) gel formation by simple 37°C incubation, with a reinforcement effect at neutralization. It facilitates processing of fibrin(ogen) materials, for coating, molding and extrusion, and offers new possibilities such as 3D printing. This approach is further compatible with type I collagen processing and can provide advanced tissue engineering scaffolds with high bioactivity.
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Preprints, Working Papers, ...
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https://hal.archives-ouvertes.fr/hal-03085797
Contributor : Lea Trichet <>
Submitted on : Tuesday, December 22, 2020 - 3:00:45 AM
Last modification on : Monday, January 4, 2021 - 12:12:04 PM

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2020.05.12.091793.full.pdf
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Clément Rieu, Gervaise Mosser, Bernard Haye, Nicolas Sanson, Thibaud Coradin, et al.. Thrombin-free polymerization leads to pure fibrin(ogen) materials with extended processing capacity. 2020. ⟨hal-03085797⟩

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