A mineral provides the template: peptides assemble into arrays of flat nanotapes on mica surfaces
The work itself was done primarily by Conor Whitehouse, working in a group headed by Neville Boden. This group have been learning in recent years how to make small peptides, which, above a particular concentration in solution, have the unique ability to spontaneously self-assemble into long tape-like aggregates a single molecule in thickness-reminiscent of pieces of tagliatelle. These small tagliatelle are twisted and this causes them to intertwine each other and stack into more complex fibrils that look just like pieces of fusili.
Surprising things happen when a solution containing single, isolated molecules of these peptides is deposited onto a muskovite surface. Muskovite is a mica, a scaly mineral with a pearlescent shine. Here the peptide molecules undergo side-by-side self-assembly into elongated, flattened, tapes. The tapes only grow in length until they bump into another tape, which results in a "monolayer". "Thus, the tapes are not twisted as they are in solution; instead, they lie flat on the surface," reports Whitehouse. "They have to untwist themselves, which they do when the binding energy between the peptide and the mica is high enough," says Whitehouse, "what holds the tapes on the mica appears to be an electrostatic attraction between charged groups in the peptides and oppositely charged ions in the crystal lattice."
When in contact with solution, the tapes have a hexagonal arrangement reflecting the symmetry of the mica surface. However, when the solvent is carefully removed, the organization of the tapes on the surface changes dramatically. "We can thus obtain densely packed monolayers of tapes with an extended parallel organization," says Whitehouse, "this is practically important because it enables surface coatings to be made into which protein-like functionality could be incorporated."
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