RT Journal Article
SR Electronic
T1 Thrombin-free polymerization leads to pure fibrin(ogen) materials with extended processing capacity
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.05.12.091793
DO 10.1101/2020.05.12.091793
A1 Clément Rieu
A1 Gervaise Mosser
A1 Bernard Haye
A1 Nicolas Sanson
A1 Thibaud Coradin
A1 Léa Trichet
YR 2020
UL http://biorxiv.org/content/early/2020/05/14/2020.05.12.091793.abstract
AB 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.Competing Interest StatementThe authors have declared no competing interest.