Fig. 2: Constructing DSPG by molecular-level co-assembly strategy.

a Schematic of the bioinspired design and assembly process. Green circle, the chemical bond between SFD. Purple circle, the chemical bond between SFD and HASH. Created in BioRender. Dong, H. (https://BioRender.com/1sendhs). b Microstructure changes of SFD, SFDHS and DSPG observed by TEM. Scale bar, 100 nm (SFD and SFDHS); 500 nm (DSPG). Created in BioRender. Dong, H. (https://BioRender.com/tqwo99r). c AFM images of SFD, SFDHS and DSPG. Scale bar, 200 nm. d ζ-potential of SF, SFD, and HASH. Error bars represent standard deviation. n = 3 independent replicates. e Thioflavin T staining fluorescence intensity during assembly. Error bars represent standard deviation. n = 4 independent replicates. (nsp = 0.639, nsp = 0.998, ***p = 3.41 ×10-10, ***p = 3.05 ×10-10). f CD spectrum and secondary structure analysis. g Effective Young’s Modulus measured by nanoindentation. Error bars represent standard deviation. n = 3 independent replicates. (*p = 0.016). h Schematic of the lyophilization process for fabricating sponge-like DSPG. Created in BioRender. Dong, H. (https://BioRender.com/57mxl3c). i Swelling ratio and dimensional changes of sponge-like SPG and DSPG. Error bars represent standard deviation, n = 3 independent replicates. j Stress values of SPG and DSPG at 75% strain. Error bars represent standard deviation. n = 3 independent replicates. (*p = 0.014). k Cyclic compression curve of DSPG. l1–l4 Fourier self-deconvolution (FSD) analysis of protein secondary structures in SPG and DSPG, with pie charts illustrating the proportions of different secondary structures. m Radar chart evaluating storage modulus, loss modulus, porosity, swelling ratio, degradation rate, and deformation ratio of DSPGs with varying SFD/HASH ratios. Statistical analyses were performed with one-way ANOVA, followed by Tukey’s multiple comparison post hoc test, *p < 0.05, ** p < 0.01 and *** p < 0.001. Source data are provided as a Source Data file.