Conformation-driven strategy for resilient and functional protein materials

Proc Natl Acad Sci U S A. 2022 Jan 25;119(4):e2115523119. doi: 10.1073/pnas.2115523119.

Abstract

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.

Keywords: conformation; elasticity; polymorphism; protein; silk.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Fibroins / chemistry
  • Models, Molecular*
  • Protein Conformation*
  • Proteins / chemistry*
  • Spectrum Analysis
  • Structure-Activity Relationship

Substances

  • Proteins
  • Fibroins