ArticleSmall science2024
Innovative Self-Assembly of 15-Mer Chimeric α-Peptide-Oligourea Foldamers toward Cl
Article in Small science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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13 authors.
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Abstract
Constructing artificial ion channels is a challenging task. Herein, the de novo design of transmembrane ion channels made up of amphiphilic peptide-oligourea chimeric helices is described. They consist of an oligourea segment (7-mer) attached to the C-terminus of a short peptide (8-mer). Mass spectrometry (MS) and transmission electron microscopy (TEM) analyses show that in an aqueous solution, two of these chimeras (HPU-E and HPU-N) independently form defined oligomeric structures. TEM also shows that they form fiber bundles. The third related chimera HPU-F does not oligomerize (MS) but forms spherical nanostructures (TEM). HPU-E and HPU-N exhibit anion transport activity across lipid bilayers via antiport mechanism (HPU-N > HPU-E). The anion selectivity of HPU-N is Cl
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