Metal-Directed Self-Assembly of Minimal Heterochiral Peptides into Metallo-Supramolecular β-Helical Tubules for Artificial Transmembrane Water Channels DOI

Salil Pophali,

Dandan Su,

Rudra Ata

et al.

Journal of the American Chemical Society, Journal Year: 2025, Volume and Issue: unknown

Published: May 11, 2025

Transmembrane selective transport of metabolites controls essential biological functions. During the last two decades, artificial channels have been developed and cyclic peptides emerged as ideal platforms for efficient ion, sugar, nucleic acid channel translocation. Despite these tremendous developments, eluded water transport. Herein, we report formation narrow β-helical tubules with diameters ranging from 2.80 to 3.25 Å that selectively control translocation, akin natural aquaporin channels. The tubular assemblies resulted metal-driven folding assembly minimal heterochiral metal-binding 3-pyridyl-terminated peptides. bent ultrashort peptide ligand coordinates Ag+ metal ions in a head-to-tail manner, which undergoes subsequent polymerization into structure stabilized by interstrand hydrogen bonds (H-bonds) between β-strands π-π staking interactions terminal pyridyl moieties. Furthermore, sequence engineering ion coordination tailored enabled distinct synthetic double β-barrel assemblies, molecules encapsulated hydrophilic core tubes. These water-encapsulated tubes were further explored lipid bilayers. Our findings suggest such achieve single-channel permeability 106 molecules/second/channel, is within 1-2 orders magnitude lower than aquaporins, rather good ability sterically reject prevent proton present significant potential membranes purification separation sciences.

Language: Английский

Metal-Directed Self-Assembly of Minimal Heterochiral Peptides into Metallo-Supramolecular β-Helical Tubules for Artificial Transmembrane Water Channels DOI

Salil Pophali,

Dandan Su,

Rudra Ata

et al.

Journal of the American Chemical Society, Journal Year: 2025, Volume and Issue: unknown

Published: May 11, 2025

Transmembrane selective transport of metabolites controls essential biological functions. During the last two decades, artificial channels have been developed and cyclic peptides emerged as ideal platforms for efficient ion, sugar, nucleic acid channel translocation. Despite these tremendous developments, eluded water transport. Herein, we report formation narrow β-helical tubules with diameters ranging from 2.80 to 3.25 Å that selectively control translocation, akin natural aquaporin channels. The tubular assemblies resulted metal-driven folding assembly minimal heterochiral metal-binding 3-pyridyl-terminated peptides. bent ultrashort peptide ligand coordinates Ag+ metal ions in a head-to-tail manner, which undergoes subsequent polymerization into structure stabilized by interstrand hydrogen bonds (H-bonds) between β-strands π-π staking interactions terminal pyridyl moieties. Furthermore, sequence engineering ion coordination tailored enabled distinct synthetic double β-barrel assemblies, molecules encapsulated hydrophilic core tubes. These water-encapsulated tubes were further explored lipid bilayers. Our findings suggest such achieve single-channel permeability 106 molecules/second/channel, is within 1-2 orders magnitude lower than aquaporins, rather good ability sterically reject prevent proton present significant potential membranes purification separation sciences.

Language: Английский

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