Letters to Nature

Nature 430, 764-768 (12 August 2004) | doi:10.1038/nature02770; Received 11 February 2004; Accepted 16 June 2004

Self-assembly of amphiphilic dendritic dipeptides into helical pores

Virgil Percec1, Andrés E. Dulcey1, Venkatachalapathy S. K. Balagurusamy1,2, Yoshiko Miura1, Jan Smidrkal1, Mihai Peterca1,2, Sami Nummelin1, Ulrica Edlund1, Steven D. Hudson3, Paul A. Heiney2, Hu Duan3, Sergei N. Magonov4 & Sergei A. Vinogradov5

  1. Roy & Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6323, USA
  2. Department of Physics and Astronomy, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6396, USA
  3. National Institute of Standards and Technology, Gaithersburg, Maryland 20899-8544, USA
  4. Digital Instruments, Veeco Metrology Group, Santa Barbara, California 93110, USA
  5. Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6059, USA

Correspondence to: Virgil Percec1 Email: percec@sas.upenn.edu

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.