title: Membrane-targeted self-assembling cyclic peptide nanotubes.
abstract: 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 (Ca(2+)) 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.
authors.forename: Nuria
authors.initials: N
authors.lastname: Rodríguez-Vázquez
authors.forename: H Lionel
authors.initials: HL
authors.lastname: Ozores
authors.forename: Arcadio
authors.initials: A
authors.lastname: Guerra
authors.forename: Eva
authors.initials: E
authors.lastname: González-Freire
authors.forename: Alberto
authors.initials: A
authors.lastname: Fuertes
authors.forename: Michele
authors.initials: M
authors.lastname: Panciera
authors.forename: Juan M
authors.initials: JM
authors.lastname: Priegue
authors.forename: Juan
authors.initials: J
authors.lastname: Outeiral
authors.forename: Javier
authors.initials: J
authors.lastname: Montenegro
authors.forename: Rebeca
authors.initials: R
authors.lastname: Garcia-Fandino
authors.forename: Manuel
authors.initials: M
authors.lastname: Amorin
authors.affiliation: Departamento de Quimica Organica, Centro Singular de Investigacion en Quimica Biologica y Materiales Moleculares, Campus Vida, Universidad de Santiago, 15782 Santiago de Compostela, Spain. juanr.granja@usc.es.
authors.forename: Juan R
authors.initials: JR
authors.lastname: Granja
mesh_terms: D000890:Anti-Infective Agents / Q000737:chemistry* / Q000494:pharmacology; D002264:Carboxylic Acids / Q000737:chemistry; D002462:Cell Membrane / Q000737:chemistry / Q000187:drug effects; D003516:Cycloparaffins / Q000737:chemistry; D004926:Escherichia coli / Q000187:drug effects / Q000254:growth & development; D057927:Hydrophobic and Hydrophilic Interactions; D007473:Ion Channels / Q000737:chemistry* / Q000494:pharmacology; D017136:Ion Transport; D043942:Nanotubes / Q000737:chemistry* / Q000633:toxicity; D010456:Peptides, Cyclic / Q000737:chemistry*; D052899:Pore Forming Cytotoxic Proteins / Q000737:chemistry* / Q000494:pharmacology; D013211:Staphylococcus aureus / Q000187:drug effects / Q000254:growth & development; D044445:Ulva / Q000187:drug effects / Q000254:growth & development
chemical_list: D000890:Anti-Infective Agents; D002264:Carboxylic Acids; D003516:Cycloparaffins; D007473:Ion Channels; D010456:Peptides, Cyclic; D052899:Pore Forming Cytotoxic Proteins