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* Department of Chemistry and Biochemistry, and
Communicated by Paul D. Boyer, University of California, Los
Angeles, CA, December 22, 2000 (received for review November 9, 2000)
A general strategy is described for designing proteins that self
assemble into large symmetrical nanomaterials, including molecular
cages, filaments, layers, and porous materials. In this strategy, one
molecule of protein A, which naturally forms a self-assembling oligomer, An, is fused rigidly to one molecule of protein
B, which forms another self-assembling oligomer, Bm. The
result is a fusion protein, A-B, which self assembles with other
identical copies of itself into a designed nanohedral particle or
material, (A-B)p. The strategy is demonstrated through the
design, production, and characterization of two fusion proteins: a
49-kDa protein designed to assemble into a cage approximately 15 nm
across, and a 44-kDa protein designed to assemble into long filaments
approximately 4 nm wide. The strategy opens a way to create a wide
variety of potentially useful protein-based materials, some of which
share similar features with natural biological assemblies.
Applied Biological Sciences
Nanohedra: Using symmetry to design self assembling protein
cages, layers, crystals, and filaments
,
,
,
, and
,§
Department of Energy Laboratory of Structural Biology
and Molecular Medicine, University of California, Los Angeles, CA
90095-1569
J.E.P. and C.C. contributed equally to this work.
www.pnas.org/cgi/doi/10.1073/pnas.041614998
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