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Article

pH-Responsive Self-Assembly of Designer Aromatic Peptide Amphiphiles and Enzymatic Post-Modification of Assembled Structures

1
Department of Applied Chemistry, School of Engineering, Kyushu University, Fukuoka 819-0395, Japan
2
Center for Future Chemistry, Kyushu University, Fukuoka 819-0395, Japan
*
Authors to whom correspondence should be addressed.
These authors equally contributed to this work.
Academic Editor: Ayae Sugawara-Narutaki
Int. J. Mol. Sci. 2021, 22(7), 3459; https://doi.org/10.3390/ijms22073459
Received: 28 February 2021 / Revised: 23 March 2021 / Accepted: 25 March 2021 / Published: 27 March 2021
(This article belongs to the Special Issue Self-Assembly Mechanism and Connection of Peptides and Proteins)
Supramolecular fibrous materials in biological systems play important structural and functional roles, and therefore, there is a growing interest in synthetic materials that mimic such fibrils, especially those bearing enzymatic reactivity. In this study, we investigated the self-assembly and enzymatic post-modification of short aromatic peptide amphiphiles (PAs), Fmoc-LnQG (n = 2 or 3), which contain an LQG recognition unit for microbial transglutaminase (MTG). These aromatic PAs self-assemble into fibrous structures via π-π stacking interactions between the Fmoc groups and hydrogen bonds between the peptides. The intermolecular interactions and morphologies of the assemblies were influenced by the solution pH because of the change in the ionization states of the C-terminal carboxy group of the peptides. Moreover, MTG-catalyzed post-modification of a small fluorescent molecule bearing an amine group also showed pH dependency, where the enzymatic reaction rate was increased at higher pH, which may be because of the higher nucleophilicity of the amine group and the electrostatic interaction between MTG and the self-assembled Fmoc-LnQG. Finally, the accumulation of the fluorescent molecule on these assembled materials was directly observed by confocal fluorescence images. Our study provides a method to accumulate functional molecules on supramolecular structures enzymatically with the morphology control. View Full-Text
Keywords: self-assembly; peptide amphiphile; enzymatic reaction; pH-responsiveness; post-modification self-assembly; peptide amphiphile; enzymatic reaction; pH-responsiveness; post-modification
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MDPI and ACS Style

Wakabayashi, R.; Higuchi, A.; Obayashi, H.; Goto, M.; Kamiya, N. pH-Responsive Self-Assembly of Designer Aromatic Peptide Amphiphiles and Enzymatic Post-Modification of Assembled Structures. Int. J. Mol. Sci. 2021, 22, 3459. https://doi.org/10.3390/ijms22073459

AMA Style

Wakabayashi R, Higuchi A, Obayashi H, Goto M, Kamiya N. pH-Responsive Self-Assembly of Designer Aromatic Peptide Amphiphiles and Enzymatic Post-Modification of Assembled Structures. International Journal of Molecular Sciences. 2021; 22(7):3459. https://doi.org/10.3390/ijms22073459

Chicago/Turabian Style

Wakabayashi, Rie, Ayato Higuchi, Hiroki Obayashi, Masahiro Goto, and Noriho Kamiya. 2021. "pH-Responsive Self-Assembly of Designer Aromatic Peptide Amphiphiles and Enzymatic Post-Modification of Assembled Structures" International Journal of Molecular Sciences 22, no. 7: 3459. https://doi.org/10.3390/ijms22073459

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