Fig. 1: Preparation and characterizations of FgC6 patch. | Nature Communications

Fig. 1: Preparation and characterizations of FgC6 patch.

From: Molecular self-assembly strategy tuning a dry crosslinking protein patch for biocompatible and biodegradable haemostatic sealing

Fig. 1

a Hydrophobic groups were grafted onto lysine residues of Fg molecule, which were demonstrated the protein structure by using PYMOL. The hydrophobic groups were marked with green color. b Photograph illustrating the gelation of FgC6 induced by hydrophobic interaction. c Complex viscosity corresponding to the Fg and FgC6 systems, respectively. d Rheological analysis of Fg and FgC6 systems, respectively (n = 3 independent experiments). e Low magnification (2600×) and high magnification (73000×) cryogenic transmission electron microscopy (cryo-TEM) images of the Fg and FgC6 systems, respectively. In the FgC6 hydrogel, fibers are observed, formed through protein self-assembly. This contrasts with the homogeneously dispersed protein in the Fg solution. The experiment was repeated two times independently with similar results. f Synchrotron small-angle X-ray scattering (SAXS) patterns and g curves for Fg solution and FgC6 hydrogel systems. Intensity color bar (arb. units). h Fibrinopeptide A (FpA) and fibrinopeptide B (FpB) were cleaved by thrombin from Fg and FgC6 systems at a low concentration (10 mg/mL), respectively (n = 3 independent samples). i Photograph of Fg powder and FgC6 patch. Error bars, mean ± SD. P values are determined by two-sided Student’s t-test for h; ns: not significant.

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