Cyclic γ-Peptides With Transmembrane Water Channel Properties

Jie Chen; Qiang Li; Pengchao Wu; Juan Liu; Dan Wang; Xiaohong Yuan; Renlin Zheng; Rongqin Sun; Liangchun Li

doi:10.3389/fchem.2020.00368

Cyclic γ-Peptides With Transmembrane Water Channel Properties

Front Chem. 2020 Apr 30:8:368. doi: 10.3389/fchem.2020.00368. eCollection 2020.

Authors

Jie Chen¹, Qiang Li¹, Pengchao Wu¹, Juan Liu¹, Dan Wang¹, Xiaohong Yuan¹, Renlin Zheng¹, Rongqin Sun², Liangchun Li¹

Affiliations

¹ School of Life Science and Engineering, Southwest University of Science and Technology, Mianyang, China.
² School of Materials Science and Engineering, Southwest University of Science and Technology, Mianyang, China.

Abstract

Self-assembling peptides can be used to design new materials for medical and biological applications. Here we synthesized and characterized two novel cyclic γ-peptides (γ-CPs) with hydrophobic inner surfaces. The NMR and FT-IR studies confirmed that the CPs could self-assemble into parallel stacking structures via intermolecular H-bonds and π-π interactions. The morphologies of the self-assembly CPs showed bundles of nanotubes via transmission electron microscopy (TEM); these nanotubes form water channels to transport water across the lipid membrane. The properties of blocking the transport of protons like natural water channels showed that the hydrophobic inner surfaces are important in artificial transmembrane water channel designs. These studies also showed that water transport was a function of pore size and length of the assemblies.

Keywords: cyclic peptide; hydrophobic inner cavity; nanotube; self-assembling; water channels.