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    Rational Design and Self-Assembly of Coiled-Coil Linked SasG Protein Fibrils

    Year: 2020

    Journal: ACS Synth. Biol., Volume 9, JUL 17, page 1599–1607

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

    Keywords: nanorods; fibrils; protein engineering SasG; self-assembly

    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.
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