Noble Jesus, C;
Evans, R;
Forth, J;
Estarellas, C;
Gervasio, FL;
Battaglia, G;
(2021)
Amphiphilic Histidine-Based Oligopeptides Exhibit pH-Reversible Fibril Formation.
ACS Macro Letters
, 10
(8)
pp. 984-989.
10.1021/acsmacrolett.1c00142.
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Abstract
We report the design, simulation, synthesis, and reversible self-assembly of nanofibrils using polyhistidine-based oligopeptides. The inclusion of aromatic amino acids in the histidine block produces distinct antiparallel β-strands that lead to the formation of amyloid-like fibrils. The structures undergo self-assembly in response to a change in pH. This creates the potential to produce well-defined fibrils for biotechnological and biomedical applications that are pH-responsive in a physiologically relevant range.
| Type: | Article |
|---|---|
| Title: | Amphiphilic Histidine-Based Oligopeptides Exhibit pH-Reversible Fibril Formation |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1021/acsmacrolett.1c00142 |
| Publisher version: | https://doi.org/10.1021/acsmacrolett.1c00142 |
| Language: | English |
| Additional information: | © 2021 The Authors. Published by American Chemical Society. This is an Open Access publication distributed under the terms of a Creative Commons licence (https://creativecommons.org/licenses/by/4.0/). |
| Keywords: | Self organization, Nanofibers, Peptides andproteins, Monomers, Chemical structure |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > UCL BEAMS UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences > Dept of Chemistry |
| URI: | https://discovery-pp.ucl.ac.uk/id/eprint/10131497 |
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