Monolayer wall nanotubes self-assembled from short peptide bolaamphiphiles
- PMID: 33038605
- DOI: 10.1016/j.jcis.2020.09.023
Monolayer wall nanotubes self-assembled from short peptide bolaamphiphiles
Abstract
In spite of extensive research, it remains a formidable challenge to control the dimension of the nanostructures self-assembled from short designed peptides. In this work, we show that peptide bolaamphiphiles form monolayer wall nanotubes, facilitated by the interplay between the side chain structure and hydrophobicity of the central residues. The peptide KI4K self-assembles into nanotubes with a width of ~ 100 nm, but changes in the molecular structure of amino acid side chains could hugely impact the nanostructures formed. The three variants of KI4K, via the substitution of aromatic amino acids (F, Y, and Dopa) for the I residue closest to the C-terminus, could substantially reduce nanotube diameters, indicating a significant steric hindrance of the benzene rings on the lateral packing of β-sheets. However, the introduction of hydroxyl groups on the benzene rings alleviates the steric effect, with nanotube diameter increasing in the order of KI3FK, KI3YK, and KI3DopaK, suggesting the formation of side chain H-bonds between β-sheets in addition to hydrophobic contacts. Because the self-assembly process of KI3DopaK nanotubes is slow, key intermediates and their structural details are well characterized. With increasing incubation time, monolayered twisted ribbons and helical ribbons grow into mature KI3DopaK nanotubes via the pitch closing route.
Keywords: Formation pathway; Intermediate; Nanotube; Peptide bolaamphiphile; Self-assembly.
Copyright © 2020 Elsevier Inc. All rights reserved.
Conflict of interest statement
Declaration of Competing Interest The authors have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
Similar articles
-
Solvent Controlled Structural Transition of KI4K Self-Assemblies: from Nanotubes to Nanofibrils.Langmuir. 2015 Dec 1;31(47):12975-83. doi: 10.1021/acs.langmuir.5b02303. Epub 2015 Nov 16. Langmuir. 2015. PMID: 26540520
-
Controlling the Diameters of Nanotubes Self-Assembled from Designed Peptide Bolaphiles.Small. 2018 Mar;14(12):e1703216. doi: 10.1002/smll.201703216. Epub 2018 Feb 12. Small. 2018. PMID: 29430820
-
Unraveling the mechanism of nanotube formation by chiral self-assembly of amphiphiles.J Am Chem Soc. 2011 Mar 2;133(8):2511-7. doi: 10.1021/ja107069f. Epub 2011 Jan 18. J Am Chem Soc. 2011. PMID: 21244023
-
Self-Assembling Peptidic Bolaamphiphiles for Biomimetic Applications.ACS Biomater Sci Eng. 2021 Aug 9;7(8):3545-3572. doi: 10.1021/acsbiomaterials.1c00576. Epub 2021 Jul 26. ACS Biomater Sci Eng. 2021. PMID: 34309378 Review.
-
Membrane-targeted self-assembling cyclic peptide nanotubes.Curr Top Med Chem. 2014;14(23):2647-61. doi: 10.2174/1568026614666141215143431. Curr Top Med Chem. 2014. PMID: 25515753 Review.
Cited by
-
Self-Assembly of Short Amphiphilic Peptides and Their Biomedical Applications.Curr Pharm Des. 2022;28(44):3546-3562. doi: 10.2174/1381612829666221124103526. Curr Pharm Des. 2022. PMID: 36424793 Review.
-
Theoretical investigation of tube-like supramolecular structures formed through bifurcated lithium bonds.Sci Rep. 2023 Sep 14;13(1):15260. doi: 10.1038/s41598-023-41979-5. Sci Rep. 2023. PMID: 37709798 Free PMC article.
-
Cell Adhesion Motif-Functionalized Lipopeptides: Nanostructure and Selective Myoblast Cytocompatibility.Biomacromolecules. 2023 Jan 9;24(1):213-224. doi: 10.1021/acs.biomac.2c01068. Epub 2022 Dec 15. Biomacromolecules. 2023. PMID: 36520063 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources