Self-assembling peptide nanotubes from enantiomeric pairs of cyclic peptides with alternating D and L amino acid residues

Cyclic peptides with alternating d- and l-amino acid residues containing tert-leucine residues in every second position can form peptide nanotubes only when both enantiomers of the peptide are present in the solution. These results strongly indicate the formation of peptide nanotubes that assemble with one enantiomer in every second position, thereby forming a lamellar structure. Copyright © 2004 American Chemical Society.