Innovative Self‐Assembly of 15‐Mer Chimeric α‐Peptide–Oligourea Foldamers toward Cl−‐Selective Ion Channels
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 spectr...
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Published in | Small science Vol. 4; no. 8 |
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Main Authors | , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Weinheim
John Wiley & Sons, Inc
01.08.2024
Wiley Wiley-VCH |
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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−>NO3− > Br−>SCN− > I− > AcO−>F−, which can be due to anion binding within the channels rather than size exclusion. Patch‐clamp data support HPU‐N's Cl− selectivity (PCl−/PI− = 3.26). X‐ray crystal structure (1.77 Å) of HPU‐N reveals well‐packed α‐helices, and cryo‐electron microscopy data shows the formation of nanotubes (13.7 Å diameter pores) and transmembrane channels. The study shows that α‐peptide–oligourea‐based de novo design can yield unique bioactive molecules with defined structures and functions.
Chimeric foldamers synthesized by linking an α‐peptide to the N‐terminus of an oligourea possess distinct hydrophobic and hydrophilic faces. Two such foldamers exhibit fiber‐like self‐assembly and demonstrate high anion transport activity in lipid bilayers. The quaternary structure from X‐ray crystallography revealed helical bundles and hydrophilic pores of ≈20 Å diameter. Cryo‐EM of liposome‐embedded chimera demonstrated self‐assembled channel‐like structures. |
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AbstractList | 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−>NO3− > Br−>SCN− > I− > AcO−>F−, which can be due to anion binding within the channels rather than size exclusion. Patch‐clamp data support HPU‐N's Cl− selectivity (PCl−/PI− = 3.26). X‐ray crystal structure (1.77 Å) of HPU‐N reveals well‐packed α‐helices, and cryo‐electron microscopy data shows the formation of nanotubes (13.7 Å diameter pores) and transmembrane channels. The study shows that α‐peptide–oligourea‐based de novo design can yield unique bioactive molecules with defined structures and functions. 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 − >NO 3 − > Br − >SCN − > I − > AcO − >F − , which can be due to anion binding within the channels rather than size exclusion. Patch‐clamp data support HPU‐N's Cl − selectivity (PCl − /PI − = 3.26). X‐ray crystal structure (1.77 Å) of HPU‐N reveals well‐packed α‐helices, and cryo‐electron microscopy data shows the formation of nanotubes (13.7 Å diameter pores) and transmembrane channels. The study shows that α‐peptide–oligourea‐based de novo design can yield unique bioactive molecules with defined structures and functions. 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−>NO3− > Br−>SCN− > I− > AcO−>F−, which can be due to anion binding within the channels rather than size exclusion. Patch‐clamp data support HPU‐N's Cl− selectivity (PCl−/PI− = 3.26). X‐ray crystal structure (1.77 Å) of HPU‐N reveals well‐packed α‐helices, and cryo‐electron microscopy data shows the formation of nanotubes (13.7 Å diameter pores) and transmembrane channels. The study shows that α‐peptide–oligourea‐based de novo design can yield unique bioactive molecules with defined structures and functions. Chimeric foldamers synthesized by linking an α‐peptide to the N‐terminus of an oligourea possess distinct hydrophobic and hydrophilic faces. Two such foldamers exhibit fiber‐like self‐assembly and demonstrate high anion transport activity in lipid bilayers. The quaternary structure from X‐ray crystallography revealed helical bundles and hydrophilic pores of ≈20 Å diameter. Cryo‐EM of liposome‐embedded chimera demonstrated self‐assembled channel‐like structures. |
Author | Collie, Gavin W. Luo, Min Dutta, Chiranjit Fan, Jingsong Barboiu, Mihail Guichard, Gilles Kumar, Prakash Pasco, Morgane Krishnamurthy, Pannaga Li, Jianwei Su, Dandan Kini, R. Manjunatha Yoo, Sung Hyun |
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Snippet | Constructing artificial ion channels is a challenging task. Herein, the de novo design of transmembrane ion channels made up of amphiphilic peptide–oligourea... Constructing artificial ion channels is a challenging task. Herein, the de novo design of transmembrane ion channels made up of amphiphilic peptide–oligourea... |
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SubjectTerms | Aqueous solutions Chemical Sciences Chloride Design foldamers helices ion channels lipid membranes Lipids Mass spectrometry Membranes Microscopy Peptides Scientific imaging self‐assembly structure |
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Title | Innovative Self‐Assembly of 15‐Mer Chimeric α‐Peptide–Oligourea Foldamers toward Cl−‐Selective Ion Channels |
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