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 (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.
Current Topics in Medicinal Chemistry
Title:Membrane-Targeted Self-Assembling Cyclic Peptide Nanotubes
Volume: 14 Issue: 23
Author(s): Nuria Rodriguez-Vazquez, H. Lionel Ozores, Arcadio Guerra, Eva Gonzalez-Freire, Alberto Fuertes, Michele Panciera, Juan M. Priegue, Juan Outeiral, Javier Montenegro, Rebeca Garcia-Fandino, Manuel Amorin and Juan R. Granja
Affiliation:
Keywords: Antimicrobials, Ion channels, Membrane, Nanotubes, peptide, Self-assembling.
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 (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.
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Rodriguez-Vazquez Nuria, Ozores Lionel H., Guerra Arcadio, Gonzalez-Freire Eva, Fuertes Alberto, Panciera Michele, Priegue M. Juan, Outeiral Juan, Montenegro Javier, Garcia-Fandino Rebeca, Amorin Manuel and Granja R. Juan, Membrane-Targeted Self-Assembling Cyclic Peptide Nanotubes, Current Topics in Medicinal Chemistry 2014; 14 (23) . https://dx.doi.org/10.2174/1568026614666141215143431
DOI https://dx.doi.org/10.2174/1568026614666141215143431 |
Print ISSN 1568-0266 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4294 |
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