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464 Designing supramolecular protein assemblies Todd O Yeates* and Jennifer E Padilla Many natural proteins self-assemble, either to fulfill their D- and L-amino acids) that self-assembled to form filaments. biological function or as part of a pathogenic process. Several variations on this theme have been explored as Biological assembly phenomena such as amyloidogenesis, well [15–18,19?,20]. Here, we review recent work on linear domain swapping and symmetric oligomerization are inspiring assemblies built from proteins or polypeptides containing new strategies for designing proteins that self-assemble to the natural L-amino acids. form supramolecular complexes. Recent advances include the design of novel proteins that assemble into filaments, β-Sheet peptides and amyloid symmetric cages and regular arrays. β-Sheet proteins, and amyloid proteins in particular, have served as useful guides in designing self-assembling Addresses proteins. The innate hydrogen-bonding pattern of β strands UCLA Department of Chemistry and Biochemistry, and UCLA and β sheets leads naturally to unbounded assemblies, Department of Energy Center for Genomics and Proteomics, especially linear fibrils (Figure 1a). This tendency is well 611 Charles E Young Drive East, University of California, Los Angeles, illustrated by the behavior of designed β-sheet proteins Los Angeles, California 90095-1569, USA *e-mail: yeates@mbi.ucla.edu that self-assembled unexpectedly into amyloid-like fibrils [21,22?] and by the creation of a combinatorial library of Current Opinion in Structural Biology 2002, 12:464–470 β-sheet proteins, all of which assembled into fibrils [23]. 0959-440X/02/$ — see front matter Amyloid-like fibrils have also been created fr