Peptide nanotubes are novel supramolecular nanobiomaterials that have a tubular structure. The
stacking of cyclic components is one of the most promising strategies amongst the methods described in recent
years for the preparation of nanotubes. This strategy allows precise control of the nanotube surface
properties and the dimensions of the tube diameter. In addition, the incorporation of 3-
aminocycloalkanecarboxylic acid residues in the nanotube-forming peptides allows control of the internal
properties of the supramolecular tube. The research aimed at the application of membrane-interacting self-assembled cyclic
peptide nanotubes (SCPNs) is summarized in this review. The cyclic peptides are designed to interact with phospholipid
bilayers to induce nanotube formation. The properties and orientation of the nanotube can be tuned by tailoring the
peptide sequence. Hydrophobic peptides form transmembrane pores with a hydrophilic orifice, the nature of which has
been exploited to transport ions and small molecules efficiently. These synthetic ion channels are selective for alkali metal
ions (Na+, K+ or Cs+) over divalent cations (Ca2+) or anions (Cl-). Unfortunately, selectivity was not achieved within the
series of alkali metal ions, for which ion transport rates followed the diffusion rates in water. Amphipathic peptides form
nanotubes that lie parallel to the membrane. Interestingly, nanotube formation takes place preferentially on the surface of
bacterial membranes, thus making these materials suitable for the development of new antimicrobial agents.
Keywords: Antimicrobials, Ion channels, Membrane, Nanotubes, peptide, Self-assembling.
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