Differential contributions of conformation extension and domain unfolding to properties of fibronectin nanotextiles

Nano Lett. 2012 Nov 14;12(11):5587-92. doi: 10.1021/nl302643g. Epub 2012 Oct 8.

Abstract

Fibronectin (FN) textiles are built as nanometer-thick fabrics. When uniaxially loaded, these fabrics exhibit a distinct threshold between elastic and plastic deformation with increasing stretch. Fabric mechanics are modeled using an eight-chain network and two-state model, revealing that elastic properties of FN depend on conformational extension of the protein and that plastic deformation depends on domain unfolding. Our results suggest how the molecular architecture of a molecule can be exploited for designer mechanical properties of a bulk material.

Publication types

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

MeSH terms

  • Dimerization
  • Elasticity
  • Extracellular Matrix / metabolism
  • Fibronectins / chemistry*
  • Models, Statistical
  • Molecular Conformation
  • Optics and Photonics
  • Protein Denaturation
  • Protein Folding
  • Protein Structure, Tertiary
  • Textiles

Substances

  • Fibronectins