Rational design and self-assembly of coiled-coil linked sasG protein fibrils

Lukas Jasaitis, Callum D. Silver, Andrea E. Rawlings, Daniel T. Peters, Fiona Whelan, Lynne Regan, Laia Pasquina-Lemonche, Jennifer R. Potts, Steven D. Johnson, Sarah S. Staniland*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Protein engineering is an attractive approach for the self-assembly of nanometer-scale architectures for a range of potential nanotechnologies. Using the versatile chemistry provided by protein folding and assembly, coupled with amino acid side-chain functionality, allows for the construction of precise molecular "protein origami"hierarchical patterned structures for a range of nanoapplications such as stand-alone enzymatic pathways and molecular machines. The Staphyloccocus aureus surface protein SasG is a rigid, rod-like structure shown to have high mechanical strength due to "clamp-like"intradomain features and a stabilizing interface between the G5 and E domains, making it an excellent building block for molecular self-assembly. Here we characterize a new two subunit system composed of the SasG rod protein genetically conjugated with de novo designed coiled-coils, resulting in the self-assembly of fibrils. Circular dichroism (CD) and quartz-crystal microbalance with dissipation (QCM-D) are used to show the specific, alternating binding between the two subunits. Furthermore, we use atomic force microscopy (AFM) to study the extent of subunit polymerization in a liquid environment, demonstrating self-assembly culminating in the formation of linear macromolecular fibrils.

Original languageEnglish
Pages (from-to)1599-1607
Number of pages9
JournalACS Synthetic Biology
Issue number7
Publication statusPublished - 17 Jul 2020


  • fibrils
  • nanorods
  • protein engineering
  • SasG
  • self-assembly


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