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Localized Supramolecular Peptide Self‐Assembly Directed by Enzyme‐Induced Proton Gradients
Author(s) -
Rodon Fores Jennifer,
Martinez Mendez Miguel Leonardo,
Mao Xiyu,
Wagner Déborah,
Schmutz Marc,
Rabineau Morgane,
Lavalle Philippe,
Schaaf Pierre,
Boulmedais Fouzia,
Jierry Loïc
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201709029
Subject(s) - glucose oxidase , nanoreactor , supramolecular chemistry , horseradish peroxidase , chemistry , electrode , self assembly , redox , combinatorial chemistry , nanotechnology , chemical engineering , catalysis , inorganic chemistry , materials science , organic chemistry , enzyme , molecule , engineering
Electrodes are ideal substrates for surface localized self‐assembly processes. Spatiotemporal control over such processes is generally directed through the release of ions generated by redox reactions occurring specifically at the electrode. The so‐used gradients of ions proved their effectiveness over the last decade but are in essence limited to material‐based electrodes, considerably reducing the scope of applications. Herein is described a strategy to enzymatically generate proton gradients from non‐conductive surfaces. In the presence of oxygen, immobilization of glucose oxidase (GOx) on a multilayer film provides a flow of protons through enzymatic oxidation of glucose by GOx. The confined acidic environment located at the solid–liquid interface allows the self‐assembly of Fmoc‐AA‐OH (Fmoc=fluorenylmethyloxycarbonyl and A=alanine) dipeptides into β‐sheet nanofibers exclusively from and near the surface. In the absence of oxygen, a multilayer nanoreactor containing GOx and horseradish peroxidase (HRP) similarly induces Fmoc‐AA‐OH self‐assembly.