Engineering amyloid fibrils from β-solenoid proteins for biomaterials applications

Maria D R Peralta, Arpad Karsai, Alice Ngo, Catherine Sierra, Kai T. Fong, Natha Robert Hayre, Nima Mirzaee, Krishnakumar Mayuram Ravikumar, Alexander J. Kluber, Xi Chen, Gang-yu Liu, Michael D. Toney, Rajiv R. Singh, Daniel Lee Cox

Research output: Contribution to journalArticlepeer-review

40 Scopus citations


Nature provides numerous examples of self-assembly that can potentially be implemented for materials applications. Considerable attention has been given to one-dimensional cross-β or amyloid structures that can serve as templates for wire growth or strengthen materials such as glue or cement. Here, we demonstrate controlled amyloid self-assembly based on modifications of β-solenoid proteins. They occur naturally in several contexts (e.g., antifreeze proteins, drug resistance proteins) but do not aggregate in vivo due to capping structures or distortions at their ends. Removal of these capping structures and regularization of the ends of the spruce budworm and rye grass antifreeze proteins yield micron length amyloid fibrils with predictable heights, which can be a platform for biomaterial-based self-assembly. The design process, including all-atom molecular dynamics simulations, purification, and self-assembly procedures are described. Fibril formation with the predicted characteristics is supported by evidence from thioflavin-T fluorescence, circular dichroism, dynamic light scattering, and atomic force microscopy. Additionally, we find evidence for lateral assembly of the modified spruce budworm antifreeze fibrils with sufficient incubation time. The kinetics of polymerization are consistent with those for other amyloid formation reactions and are relatively fast due to the preformed nature of the polymerization nucleus.

Original languageEnglish (US)
Pages (from-to)449-463
Number of pages15
JournalACS Nano
Issue number1
StatePublished - Jan 27 2015


  • amyloid
  • antifreeze protein
  • atomic force microscopy
  • thioflavin-T fluorescence
  • β-solenoid

ASJC Scopus subject areas

  • Engineering(all)
  • Materials Science(all)
  • Physics and Astronomy(all)


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