Self-assembling β-Sheet Tape Forming Peptides

Abstract

Biological proteins have intrinsically the ability to self-assemble, and this has been implicated in pathological situations called amyloid diseases. Conversely understanding protein self-assembly and how to control it can open up the route to new nanodevices and nanostructured materials for a wide range of applications in medicine, chemical industry and nanotechnology. Biological peptides and proteins have complex chemical structure and conformation. This makes it difficult to decipher the fundamental principles that drive their self-assembling behaviours. Here we review our work on the self-assembly of simple de novo peptides in solution. These peptides are designed so that: (i) the chemical complexity of the primary structure and (ii) the conformational complexity are both kept to a minimum. Each peptide adopts an extended β-strand conformation in solution and these β-strands self-assemble in one dimension to form elongated tapes as well as higher order aggregates with pure antiparallel β-sheet structure, without the presence of any other conformations such as turns, loops, α-helices or random coils. Experimental data of the self-assembling properties are fitted with an appropriate theoretical model to build a quantitative relationship between peptide primary structure and self-assembly. These simple systems provide us with the opportunity to reveal the generic properties of the pure β-sheet structures and expose the underlying physicochemical principles that drive the self-assembling behaviour of this biological motif.

Keywords:

• Molecular self-assembly
• Peptides
• β-Sheet
• Tapes
• Fibrils

Acknowledgements

The work summarised here has been funded by The Royal Society (Royal Society University Research Fellowship to AA) and The Engineering and Physical Sciences Research Council (EPSRC) of the United Kingdom.

Notes

^†Current address: Department of Biological Sciences, University of Warwick, Coventry, CV4 7AL, UK.

^‡Current address: Institut Charles Sadron, 6 rue Bossingault, 67083 Strasbourg Cedex, France.

^‡Current address: Institut Charles Sadron, 6 rue Bossingault, 67083 Strasbourg Cedex, France.

Additional information

Notes on contributors

A.J. Beevers

† †Current address: Department of Biological Sciences, University of Warwick, Coventry, CV4 7AL, UK.

I. Nyrkova

‡ ‡Current address: Institut Charles Sadron, 6 rue Bossingault, 67083 Strasbourg Cedex, France.

A.N. Semenov

‡ ‡Current address: Institut Charles Sadron, 6 rue Bossingault, 67083 Strasbourg Cedex, France.