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Supplementary Materials

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  • Supplementary Data
  • Supplementary Methods
  • fig. S1. SDS-PAGE of reduced fibrin gels without (Fib−) and with additional cross-linking by FXIIIa (Fib+).
  • fig. S2. Differential storage modulus measured as a function of prestrain for three different mixtures of fibrin hydrogels.
  • fig. S3. Creep recovery tests of partially cross-linked and fully cross-linked fibrin gels.
  • fig. S4. Curves showing average α helix, β sheet, and random coil content of a typical relaxed hydrogel as a function of number of pixels included in the calculation, sorted from maximum protein content (CH value) to minimum protein content.
  • fig. S5. Fibrin protein concentration under strain.
  • fig. S6. Random coil content for increasing strain in three different hydrogels.
  • fig. S7. SD of CH3 intensity (2930 cm−1) within the top 30 highest protein signal pixels normalized to the average CH3 intensity of the experiment.
  • fig. S8. Spectral maps for never loaded partially cross-linked hydrogels (7.5 mg/ml).
  • fig. S9. Images and histogram plots showing the α helix peak contribution as percent content within partially cross-linked fibrin gels at different strains.
  • fig. S10. Images and histogram plots showing the random coil peak contribution as percent content within partially cross-linked fibrin gels at different strains.
  • fig. S11. Normalized spatial autocorrelation of β sheet content maps along direction orthogonal to loading axis.
  • fig. S12. Spectral maps for 85% vertical strained cross-linked hydrogel.
  • fig. S13. Confocal fluorescence microscopy of fibrin gels with different fibrinogen concentrations (total field of view, 48 μm ? 48 μm).
  • fig. S14. Contribution of β sheets to the amide I band for increasing strain in low- and high-concentration fibrin.
  • fig. S15. SDS-PAGE of the supernatant from different hydrogels to check the complete polymerization of fibrinogen monomers.
  • fig. S16. Schematic of the BCARS microscope setup.
  • table S1. Results from creep recovery experiments for partially cross-linked and fully cross-linked fibrin.

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