Artificial ion channels formed by a synthetic cyclic peptide

The Journal of Peptide Research : Official Journal of the American Peptide Society
D WangR W Roeske

Abstract

A new cyclic peptide 1 having an (LLLD)3 configuration pattern was designed that is capable of forming artificial transmembrane ion channels by self-assembly of planar peptide rings, with hydrophilic groups arrayed in the interior of the channel. Ion permeability in the presence of the synthetic peptide 1, cyclo[-Trp-Dap-Leu-D-Ala-Trp-Ser-Val-D-Ala-Trp-Ser-Ile-Gly-] (Dap: L-diaminopropionic acid), was observed in lipid bilayer membranes. The pH dependence of ionic conductance showed that the beta-amino group of Dap may play a role in the conductance of the peptide channels. Fourier-transform infrared and circular dichroism data imply that, in a membrane, a stack of cyclic peptides is formed in which the inter peptide H bonds form a kind of beta-structure analogous to that in the gramicidin A dimer and distinct from the H-bonding pattern of the beta-barrels.

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Citations

Mar 17, 2004·Bioorganic & Medicinal Chemistry·Pinaki TalukdarStefan Matile
May 9, 2012·IET Nanobiotechnology·H Pradeep, G K Rajanikant
Oct 8, 2003·Proceedings of the National Academy of Sciences of the United States of America·Nathalie SordéStefan Matile
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Aug 10, 2012·Chemical Society Reviews·Robert ChapmanSébastien Perrier
Jun 5, 2015·Chemistry : a European Journal·Harekrushna BeheraNandita Madhavan
Aug 12, 2005·Chemical Reviews·Alma VisoAida Flores
May 4, 2021·Chemical Reviews·Qiao SongSébastien Perrier
Jul 3, 2019·Journal of the American Chemical Society·Shawn M DarnallTing Xu

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