Self-assembly and regulation of protein cages from pre-organised coiled-coil modules

Fabio Lapenta, Jana Aupič, Marco Vezzoli, Žiga Strmšek, Stefano Da Vela, Dmitri I. Svergun, José María Carazo, Roberto Melero and Roman Jerala ()
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Fabio Lapenta: National Institute of Chemistry
Jana Aupič: National Institute of Chemistry
Marco Vezzoli: University of Parma
Žiga Strmšek: National Institute of Chemistry
Stefano Da Vela: EMBL c/o DESY
Dmitri I. Svergun: EMBL c/o DESY
José María Carazo: Centro Nacional de Biotecnología (CNB-CSIC)
Roberto Melero: Centro Nacional de Biotecnología (CNB-CSIC)
Roman Jerala: National Institute of Chemistry

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: Abstract Coiled-coil protein origami (CCPO) is a modular strategy for the de novo design of polypeptide nanostructures. CCPO folds are defined by the sequential order of concatenated orthogonal coiled-coil (CC) dimer-forming peptides, where a single-chain protein is programmed to fold into a polyhedral cage. Self-assembly of CC-based nanostructures from several chains, similarly as in DNA nanotechnology, could facilitate the design of more complex assemblies and the introduction of functionalities. Here, we show the design of a de novo triangular bipyramid fold comprising 18 CC-forming segments and define the strategy for the two-chain self-assembly of the bipyramidal cage from asymmetric and pseudo-symmetric pre-organised structural modules. In addition, by introducing a protease cleavage site and masking the interfacial CC-forming segments in the two-chain bipyramidal cage, we devise a proteolysis-mediated conformational switch. This strategy could be extended to other modular protein folds, facilitating the construction of dynamic multi-chain CC-based complexes.

Date: 2021
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DOI: 10.1038/s41467-021-21184-6

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