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Transition of Nano-Architectures Through Self-Assembly of Lipidated β(3)-Tripeptide Foldamers
β(3)-peptides consisting exclusively of β(3)-amino acids adopt a variety of non-natural helical structures and can self-assemble into well-defined hierarchical structures by axial head-to-tail self-assembly resulting in fibrous materials of varying sizes and shapes. To allow control of fiber morphol...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7136582/ https://www.ncbi.nlm.nih.gov/pubmed/32296680 http://dx.doi.org/10.3389/fchem.2020.00217 |
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author | Habila, Nathan Kulkarni, Ketav Lee, Tzong-Hsien Al-Garawi, Zahraa S. Serpell, Louise C. Aguilar, Marie-Isabel Del Borgo, Mark P. |
author_facet | Habila, Nathan Kulkarni, Ketav Lee, Tzong-Hsien Al-Garawi, Zahraa S. Serpell, Louise C. Aguilar, Marie-Isabel Del Borgo, Mark P. |
author_sort | Habila, Nathan |
collection | PubMed |
description | β(3)-peptides consisting exclusively of β(3)-amino acids adopt a variety of non-natural helical structures and can self-assemble into well-defined hierarchical structures by axial head-to-tail self-assembly resulting in fibrous materials of varying sizes and shapes. To allow control of fiber morphology, a lipid moiety was introduced within a tri-β(3)-peptide sequence at each of the three amino acid positions and the N-terminus to gain finer control over the lateral assembly of fibers. Depending on the position of the lipid, the self-assembled structures formed either twisted ribbon-like fibers or distinctive multilaminar nanobelts. The nanobelt structures were comprised of multiple layers of peptide fibrils as revealed by puncturing the surface of the nanobelts with an AFM probe. This stacking phenomenon was completely inhibited through changes in pH, indicating that the layer stacking was mediated by electrostatic interactions. Thus, the present study is the first to show controlled self-assembly of these fibrous structures, which is governed by the location of the acyl chain in combination with the 3-point H-bonding motif. Overall, the results demonstrate that the nanostructures formed by the β(3)-tripeptide foldamers can be tuned via sequential lipidation of N-acetyl β(3)-tripeptides which control the lateral interactions between peptide fibrils and provide defined structures with a greater homogeneous population. |
format | Online Article Text |
id | pubmed-7136582 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71365822020-04-15 Transition of Nano-Architectures Through Self-Assembly of Lipidated β(3)-Tripeptide Foldamers Habila, Nathan Kulkarni, Ketav Lee, Tzong-Hsien Al-Garawi, Zahraa S. Serpell, Louise C. Aguilar, Marie-Isabel Del Borgo, Mark P. Front Chem Chemistry β(3)-peptides consisting exclusively of β(3)-amino acids adopt a variety of non-natural helical structures and can self-assemble into well-defined hierarchical structures by axial head-to-tail self-assembly resulting in fibrous materials of varying sizes and shapes. To allow control of fiber morphology, a lipid moiety was introduced within a tri-β(3)-peptide sequence at each of the three amino acid positions and the N-terminus to gain finer control over the lateral assembly of fibers. Depending on the position of the lipid, the self-assembled structures formed either twisted ribbon-like fibers or distinctive multilaminar nanobelts. The nanobelt structures were comprised of multiple layers of peptide fibrils as revealed by puncturing the surface of the nanobelts with an AFM probe. This stacking phenomenon was completely inhibited through changes in pH, indicating that the layer stacking was mediated by electrostatic interactions. Thus, the present study is the first to show controlled self-assembly of these fibrous structures, which is governed by the location of the acyl chain in combination with the 3-point H-bonding motif. Overall, the results demonstrate that the nanostructures formed by the β(3)-tripeptide foldamers can be tuned via sequential lipidation of N-acetyl β(3)-tripeptides which control the lateral interactions between peptide fibrils and provide defined structures with a greater homogeneous population. Frontiers Media S.A. 2020-03-31 /pmc/articles/PMC7136582/ /pubmed/32296680 http://dx.doi.org/10.3389/fchem.2020.00217 Text en Copyright © 2020 Habila, Kulkarni, Lee, Al-Garawi, Serpell, Aguilar and Del Borgo. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Chemistry Habila, Nathan Kulkarni, Ketav Lee, Tzong-Hsien Al-Garawi, Zahraa S. Serpell, Louise C. Aguilar, Marie-Isabel Del Borgo, Mark P. Transition of Nano-Architectures Through Self-Assembly of Lipidated β(3)-Tripeptide Foldamers |
title | Transition of Nano-Architectures Through Self-Assembly of Lipidated β(3)-Tripeptide Foldamers |
title_full | Transition of Nano-Architectures Through Self-Assembly of Lipidated β(3)-Tripeptide Foldamers |
title_fullStr | Transition of Nano-Architectures Through Self-Assembly of Lipidated β(3)-Tripeptide Foldamers |
title_full_unstemmed | Transition of Nano-Architectures Through Self-Assembly of Lipidated β(3)-Tripeptide Foldamers |
title_short | Transition of Nano-Architectures Through Self-Assembly of Lipidated β(3)-Tripeptide Foldamers |
title_sort | transition of nano-architectures through self-assembly of lipidated β(3)-tripeptide foldamers |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7136582/ https://www.ncbi.nlm.nih.gov/pubmed/32296680 http://dx.doi.org/10.3389/fchem.2020.00217 |
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