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Natural pore-forming proteins act as viral helical coats and transmembrane channels^,,, exhibit antibacterial activity and are used in synthetic systems, such as for reversible encapsulation or stochastic sensing. These diverse functions are intimately linked to protein structure^,,,. The close link between protein structure and protein function makes the design of synthetic mimics a formidable challenge, given that structure formation needs to be carefully controlled on all hierarchy levels, in solution and in the bulk. In fact, with few exceptions^,, synthetic pore structures capable of assembling into periodically ordered assemblies that are stable in solution and in the solid state^,,, have not yet been realized. In the case of dendrimers, covalent and non-covalent coating and assembly of a range of different structures^,, has only yielded closed columns. Here we describe a library of amphiphilic dendritic dipeptides that self …