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Fibrin is the polymerized protein responsible for the stabilizing mesh in blood coagulation. Its superior mechanical properties of being stiff or elastic if needed result from a hierarchical structure, including semiflexible single fibers as well as constituent protein restructuring. Here, we stretch and shear fibrin hydrogels to a regime where unfolding transitions of α-helical structures to β-sheet are induced and observe protein structural changes with spatially-resolved coherent Raman microscopy. We confirm the theoretically predicted orthogonal orientation of helices and sheets in strained networks. Spatially resolved structure protein maps reveal that the extent of structural transition changes with gel composition and becomes highly heterogeneous at large strain, indicative of substantial load-bearing inhomogeneity .
Mischa Bonn andSapun Parekh
"Linking macroscopic rheology with molecular structure in fibrin hydrogels using coherent anti-Stokes Raman scattering (CARS) imaging", Proc. SPIE 11656, Advanced Chemical Microscopy for Life Science and Translational Medicine 2021, 1165610 (5 March 2021); https://doi.org/10.1117/12.2583182
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Mischa Bonn, Sapun Parekh, "Linking macroscopic rheology with molecular structure in fibrin hydrogels using coherent anti-Stokes Raman scattering (CARS) imaging," Proc. SPIE 11656, Advanced Chemical Microscopy for Life Science and Translational Medicine 2021, 1165610 (5 March 2021); https://doi.org/10.1117/12.2583182