Abstract
A designed peptide amphiphile C16-KKFFVLK self-assembles into nanotubes and helical ribbons in aqueous solution at room temperature. A remarkable unwinding transition, leading to twisted tapes, is observed on heating. Nanotubes and ribbons re-form on cooling.
Highlights
Chiral self-assembly of twisted sheets and helical ribbons has been studied for systems as diverse as seed pods,[2] hexabenzocoronene derivatives,[3] zinc oxide nanobelts,[4] bile salts,[5] gemini surfactants[6] and peptides[7] among others
We have discovered that a peptide amphiphile undergoes a reversible thermal transition between a state of predominantly nanotubes and helical ribbons and twisted tapes at higher temperature
In the KKFFVLK heptapeptide sequence exploited here, the two F residues in KKFFVLK drive self-assembly through hydrophobic and p-stacking interactions.7a,b,11 Two additional lysine residues are incorporated between the hexadecanyl lipid chain and the KKFFVLK motif to promote solubility and impart amphiphilicity
Summary
A designed peptide amphiphile C16-KKFFVLK self-assembles into nanotubes and helical ribbons in aqueous solution at room temperature. A remarkable unwinding transition, leading to twisted tapes, is observed on heating.
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