Conformation-driven strategy for resilient and functional protein materials

The exceptional elastic resilience of some protein materials underlies essential biomechanical functions with broad interest in biomedical fields. However, molecular design of elastic resilience is restricted to amino acid sequences of a handful of naturally occurring resilient proteins such as resilin and elastin. Here, we exploit non-resilin/elastin sequences that adopt kinetically stabilized, random coil-dominated conformations to achieve near-perfect resilience comparable with that of resilin and elastin. We also show a direct correlation between resilience and Raman-characterized protein conformations. Furthermore, we demonstrate that metastable conformation of proteins enables the construction of mechanically graded protein materials that exhibit spatially controlled conformations and resilience. These results offer insights into molecular mechanisms of protein elastomers and outline a general conformation-driven strategy for developing resilient and functional protein materials.

Automated summary

Researchers have achieved near-perfect resilience comparable to resilin and elastin using non-resilin/elastin sequences that adopt kinetically stabilized, random coil-dominated conformations. They have also demonstrated a direct correlation between resilience and Raman-characterized protein conformations, and shown that metastable protein conformations enable the construction of mechanically graded protein materials with spatially controlled conformations and resilience. These findings provide insights into the molecular mechanisms of protein elastomers and present a general conformation-driven strategy for developing resilient and functional protein materials.