Self-assembly enhances the strength of fibers made from vimentin intermediate filament proteins

Biomacromolecules. 2014 Feb 10;15(2):574-81. doi: 10.1021/bm401600a. Epub 2014 Jan 28.

Abstract

Hagfish slime threads were recently established as a promising biomimetic model for efforts to produce ecofriendly alternatives to petroleum polymers. Initial attempts to make fibers from solubilized slime thread proteins fell short of achieving the outstanding mechanics of native slime threads. Here we tested the hypothesis that the high strength and toughness of slime threads arise from the ability of constituent intermediate filaments to undergo a stress-induced α-to-β transition. To do this, we made fibers from human vimentin proteins that were first allowed to self-assemble into 10 nm intermediate filaments. Fibers made from assembled vimentin hydrogels underwent an α-to-β transition when strained and exhibited improved mechanical performance. Our data demonstrate that it is possible to make materials from intermediate filament hydrogels and that mimicking the secondary structure of native hagfish slime threads using intermediate filament self-assembly is a promising strategy for improving the mechanical performance of biomimetic protein materials.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Formates / chemistry
  • Humans
  • Hydrogels / chemistry
  • Particle Size
  • Protein Stability
  • Protein Structure, Secondary
  • Recombinant Proteins / chemical synthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Surface Properties
  • Vimentin / chemical synthesis*
  • Vimentin / chemistry
  • Vimentin / isolation & purification

Substances

  • Formates
  • Hydrogels
  • Recombinant Proteins
  • Vimentin
  • formic acid