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TitleComputational design of bifaceted protein nanomaterials.
Journal, issue, pagesbioRxiv, Year 2024
Publish dateOct 22, 2024
AuthorsSanela Rankovic / Kenneth D Carr / Justin Decarreau / Rebecca Skotheim / Ryan D Kibler / Sebastian Ols / Sangmin Lee / Jung-Ho Chun / Marti R Tooley / Justas Dauparas / Helen E Eisenach / Matthias Glögl / Connor Weidle / Andrew J Borst / David Baker / Neil P King /
PubMed AbstractRecent advances in computational methods have led to considerable progress in the design of self-assembling protein nanoparticles. However, nearly all nanoparticles designed to date exhibit strict ...Recent advances in computational methods have led to considerable progress in the design of self-assembling protein nanoparticles. However, nearly all nanoparticles designed to date exhibit strict point group symmetry, with each subunit occupying an identical, symmetrically related environment. This limits the structural diversity that can be achieved and precludes anisotropic functionalization. Here, we describe a general computational strategy for designing multi-component bifaceted protein nanomaterials with two distinctly addressable sides. The method centers on docking pseudosymmetric heterooligomeric building blocks in architectures with dihedral symmetry and designing an asymmetric protein-protein interface between them. We used this approach to obtain an initial 30-subunit assembly with pseudo-D5 symmetry, and then generated an additional 15 variants in which we controllably altered the size and morphology of the bifaceted nanoparticles by designing extensions to one of the subunits. Functionalization of the two distinct faces of the nanoparticles with protein minibinders enabled specific colocalization of two populations of polystyrene microparticles coated with target protein receptors. The ability to accurately design anisotropic protein nanomaterials with precisely tunable structures and functions could be broadly useful in applications that require colocalizing two or more distinct target moieties.
External linksbioRxiv / PubMed:39484564 / PubMed Central
MethodsEM (single particle)
Resolution4.3 Å
Structure data

47327

9dze

EMDB-47327, PDB-9dze:
Computationally Designed Bifaceted Protein Nanomaterial pD5-14
Method: EM (single particle) / Resolution: 4.3 Å

Source
  • synthetic construct (others)
KeywordsDE NOVO PROTEIN / nanomaterial / 4 component / bifaceted / penton

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