Strong underwater adhesives made by self-assembling multi-protein nanofibres

Nat Nanotechnol. 2014 Oct;9(10):858-66. doi: 10.1038/nnano.2014.199. Epub 2014 Sep 21.


Many natural underwater adhesives harness hierarchically assembled amyloid nanostructures to achieve strong and robust interfacial adhesion under dynamic and turbulent environments. Despite recent advances, our understanding of the molecular design, self-assembly and structure-function relationships of these natural amyloid fibres remains limited. Thus, designing biomimetic amyloid-based adhesives remains challenging. Here, we report strong and multi-functional underwater adhesives obtained from fusing mussel foot proteins (Mfps) of Mytilus galloprovincialis with CsgA proteins, the major subunit of Escherichia coli amyloid curli fibres. These hybrid molecular materials hierarchically self-assemble into higher-order structures, in which, according to molecular dynamics simulations, disordered adhesive Mfp domains are exposed on the exterior of amyloid cores formed by CsgA. Our fibres have an underwater adhesion energy approaching 20.9 mJ m(-2), which is 1.5 times greater than the maximum of bio-inspired and bio-derived protein-based underwater adhesives reported thus far. Moreover, they outperform Mfps or curli fibres taken on their own and exhibit better tolerance to auto-oxidation than Mfps at pH ≥ 7.0.

Publication types

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

MeSH terms

  • Adhesiveness
  • Adhesives / chemistry*
  • Animals
  • Escherichia coli / chemistry*
  • Escherichia coli / genetics
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / ultrastructure
  • Models, Molecular
  • Mytilus / chemistry*
  • Mytilus / genetics
  • Nanofibers / chemistry*
  • Nanofibers / ultrastructure
  • Proteins / chemistry*
  • Proteins / genetics
  • Proteins / ultrastructure
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / ultrastructure
  • Water / chemistry


  • Adhesives
  • Escherichia coli Proteins
  • Proteins
  • Recombinant Fusion Proteins
  • adhesive protein, mussel
  • csgA protein, E coli
  • Water