Conformable self-assembling amyloid protein coatings with genetically programmable functionality

Sci Adv. 2020 May 20;6(21):eaba1425. doi: 10.1126/sciadv.aba1425. eCollection 2020 May.

Abstract

Functional coating materials have found broad technological applications in diverse fields. Despite recent advances, few coating materials simultaneously achieve robustness and substrate independence while still retaining the capacity for genetically encodable functionalities. Here, we report Escherichia coli biofilm-inspired protein nanofiber coatings that simultaneously exhibit substrate independence, resistance to organic solvents, and programmable functionalities. The intrinsic surface adherence of CsgA amyloid proteins, along with a benign solution-based fabrication approach, facilitates forming nanofiber coatings on virtually any surface with varied compositions, sizes, shapes, and structures. In addition, the typical amyloid structures endow the nanofiber coatings with outstanding robustness. On the basis of their genetically engineerable functionality, our nanofiber coatings can also seamlessly participate in functionalization processes, including gold enhancement, diverse protein conjugations, and DNA binding, thus enabling a variety of proof-of-concept applications, including electronic devices, enzyme immobilization, and microfluidic bacterial sensors. We envision that our coatings can drive advances in electronics, biocatalysis, particle engineering, and biomedicine.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid / chemistry
  • Amyloidogenic Proteins* / genetics
  • Amyloidogenic Proteins* / metabolism
  • Biofilms
  • Escherichia coli* / genetics
  • Escherichia coli* / metabolism
  • Gold

Substances

  • Amyloid
  • Amyloidogenic Proteins
  • Gold