Self-assembly of amphiphilic dendritic dipeptides into helical pores

Natural pore-forming proteins act as viral helical coats1 and transmembrane channels2,3,4, exhibit antibacterial activity5 and are used in synthetic systems, such as for reversible encapsulation6 or stochastic sensing7. These diverse functions are intimately linked to protein structure1,2,3,4. 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 exceptions8,9, synthetic pore structures capable of assembling into periodically ordered assemblies that are stable in solution and in the solid state10,11,12,13 have not yet been realized. In the case of dendrimers, covalent14 and non-covalent15 coating and assembly of a range of different structures15,16,17 has only yielded closed columns18. Here we describe a library of amphiphilic dendritic dipeptides that self-assemble in solution and in bulk through a complex recognition process into helical pores. We find that the molecular recognition and self-assembly process is sufficiently robust to tolerate a range of modifications to the amphiphile structure, while preliminary proton transport measurements establish that the pores are functional. We expect that this class of self-assembling dendrimers will allow the design of a variety of biologically inspired systems with functional properties arising from their porous structure.