Localized Supramolecular Peptide Self-Assembly Directed by Enzyme-Induced Proton Gradients

Article abstract of DOI:10.1002/anie.201709029

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.

Full text of DOI:10.1002/anie.201709029

A Journal of the Gesellschaft Deutscher Chemiker
Angewandte
International Edition Chemie
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Accepted Article
Title: Localized Supramolecular Peptide Self-Assembly Directed by
Enzyme-Induced Proton-Gradients
Authors: Loïc JIERRY, Jennifer Rodon Fores, Miguel Leonardo
Martinez Mendez, Xiyu Mao, Déborah Wagner, Marc
Schmutz, Morgane Rabineau, Philippe Lavalle, Pierre Schaaf,
and Fouzia Boulmedais
This manuscript has been accepted after peer review and appears as an
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of the final Version of Record (VoR). This work is currently citable by
using the Digital Object Identifier (DOI) given below. The VoR will be
published online in Early View as soon as possible and may be different
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the VoR from the journal website shown below when it is published
to ensure accuracy of information. The authors are responsible for the
content of this Accepted Article.
To be cited as: Angew. Chem. Int. Ed. 10.1002/anie.201709029
Angew. Chem. 10.1002/ange.201709029
Link to VoR: http://dx.doi.org/10.1002/anie.201709029
http://dx.doi.org/10.1002/ange.201709029

Angewandte Chemie International Edition
10.1002/anie.201709029
COMMUNICATION
Localized Supramolecular Peptide Self-Assembly Directed by
Enzyme-Induced Proton-Gradients**
[a]
[a]
[a]
[a]
Jennifer Rodon Fores, Miguel Léonardo Martinez Mendez, Xiyu Mao, Déborah Wagner, Marc
[a]
[b]
[b]
[a],[b]
[a]
Schmutz, Morgane Rabineau, Philippe Lavalle, Pierre Schaaf,*
Jierry*[a]
Fouzia Boulmedais and Loïc
Abstract: 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
generate enzymatically 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 nanofibres exclusively from and
near the surface. In the absence of oxygen, a multilayer nanoreactor
containing GOx and horseradish peroxidase (HRP) induces similarly
Fmoc-AA-OH self-assembly.
according to the features of one or several gradients.[6] This
approach is inspired from reaction-diffusion processes found in
Nature and appears as a promising way for further development
of more complex chemical systems.[7]
Among the different gradient entities studied, protons are
the most used because of their easy generation at a surface
electrode. Indeed, oxidizing water or hydroquinone for instance
leadsto the production of protons that diffuse from the electrode
to the surrounding environment, creating a confined acidic
region at the interface. In 2010, Cameron’s group described the
surface-induced self-assembly of Fmoc protected dipeptides
leading to the growth of a supramolecular hydrogel resulting in a
dense fibre network.[8] Carbazole-protected amino acids have
also been investigated for their spatially resolved self-assembly
on electrode surfaces.[ Using patterned electrodes, Payne
demonstrated the specific control in space and time of the self-
assembly of Fmoc protected phenylalanine by localized
9]
application of an electrical signal during a precise duration.[10]
A
fine electrochemical control of the proton production allowed
triggering spatially and temporally resolved multicomponent
hydrogels.[11] Surface-assisted self-assembly has also been
Self-assembly is an easy and powerful way to organize
matter from molecular to nanometer scale and beyond.[1] Spatial
and temporal control over the self-assembly process has
allowed the emergence of materials with original features
through the design of nanostructured coatings or materials
giving rise to a large scope of applications.[2,3] Currently, several
methods describe the directed initiation and growth of
supramolecular self-assembly at an interface. Most of them are
triggered by a physical external stimulus or due to a template
effect coming from a prior surface treatment of the material.
Recent investigations based on chemical gradients have
demonstrated a great potential (i) to localize precisely in space
used to developed efficient biosensors by immobilizing enzymes
[12]
and bacteria.
Thus, the efficiency of this approach is well
established but the restriction to use electrodes as surfaces
reduces considerably its range of applications. In the domain of
surface-assisted self-assembly of low molecular weight
hydrogelators (LMWH), only one alternative was described so
far, based on the introduction of sulfonic acid groups on a
surface catalysing the in situ formation of the hydrogelator.[13]
Here, we describe the self-assembly of peptides directed
by a continuous gradient of protons produced enzymatically on a
non-conductive surface. Our model system is composed of (i)
Fmoc-AA-OH (Scheme 1a), a LMWH already described as
hydrogelator under acidic conditions in solution[14,15] and (ii)
glucose oxidase (GOx), an enzyme producing protons through
the transformation of glucose in gluconic acid in the presence of
[
4]
the molecular buildup, (ii) to control the assembly evolution
over time[ and (iii) to orientate the resulting nanostructure
5]
[
a]
Jennifer Rodon Fores, Miguel Léonardo Martinez Mendes, Xiyu
Mao, Déborah Wagner, Dr. Marc Schmutz, Pr. Dr. Pierre Schaaf, Dr.
Fouzia Boulmedais and Dr. Loïc Jierry
2
O (Scheme 1b). Surface immobilization of GOx in a multilayer
Université de Strasbourg, CNRS, Institut Charles Sadron (UPR22)
film will permit the production of protons in the presence of
glucose. When Fmoc-AA-OH dipeptide diffuses toward the
interface, its C-terminal carboxylate group is protonated which
should induce spontaneously its self-assembly, solely at the
interface (Scheme 1c). The buildup of GOx-coated surfaces and
the evolution of the self-assembly process over time were
followed both by quartz crystal microbalance (QCM-D) and
attenuated total reflectance Fourier transformed infrared
spectroscopy (ATR-FTIR). The morphology of the self-
assembled architectures was investigated by atomic force
microscopy (AFM), scanning electron microscopy (SEM) and
cryo-SEM.
23 rue du Loess, BP 84047, 67034 Strasbourg Cedex 2, France.
E-mail: schaaf@unistra.fr; loic.jierry@ics-cnrs.unistra.fr
[
[
b]
Dr. Morgane Rabireau, Dr. Philippe Lavalle, Pr. Dr. Pierre Schaaf
Institut National de la Santé et de la Recherche Médicale, INSERM
Unité 1121, 11 rue Humann, 67085 Strasbourg Cedex, France,
Université de Strasbourg, Faculté de Chirurgie Dentaire,
Sainte Elisabeth 67000 Strasbourg, France.
8 rue
**]
Maëlle Cahu and Camille Damestoy is acknowledged for technical
help. We gratefully acknowledge the financial support from Agence
Nationale de la Recherche (ANR-15-CE29-0015-02), International
Center for Frontier Research in Chemistry (icFRC), Labex “Chimie
des Systèmes Complexes” (Labex CSC, PSC-016), University of
Strasbourg Institute for Advanced Study (USIAS) and Institut
Universitaire de France (IUF).
Supporting information for this article is given via a link at the end of
the document.
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Angewandte Chemie International Edition
10.1002/anie.201709029
COMMUNICATION
(
Figure 1c). After 40 min, the solution was replaced by the buffer
a.
solution (rinsing step) and the normalized frequency shift
a.
c.
Fmoc-AA-OH Rinsing steps
solution
Fmoc-AA-OH
0
b.
-50
Rinsing step
Without
glucose
With
glucose
-100
β-D-Glucose
D-Gluconolactone
D-Gluconic acid
b. Multilayer film architecture
-150
PAH
GOx or BSA
0
20
40
60
c.
̴8 nm
Time (min)
Fmoc-AA-O-
Fmoc-AA-OH
(PSS/PAH)
2
PEI
Surface
Enzymes
Glucose
H+
containing
multiayer film
Figure 1. (a) Upside down vial gelation tests of Fmoc-AA-OH in the presence
of GOx; (b) Architecture of (GOx/PAH) and (BSA/PAH) films; (c) Evolution of
the normalized frequency shift (QCM-D) over time during the contact of Fmoc-
AA-OH/glucose solution (500 µL/min) with (GOx/PAH) (blue line), with
BSA/PAH) film (red dashed line) and during the contact of Fmoc-AA-OH
solution (without glucose) with a (GOx/PAH) film (green dotted line).
1
1
1
Supramolecular
hydrogel
(
1
1
increased slightly until it stabilized at around -120 Hz. In addition,
-6
the dissipation value at 15 MHz was of the order of 40 × 10 in
agreement with the formation of a hydrogel (Figure S4).
Replacing GOx in the multilayer film by bovine serum albumin
(
BSA, Mw ~ 66 kDa, IP 4.7 at 25°C) or removing glucose from
Scheme 1. (a) Chemical structure of Fmoc-AA-OH dipeptide; (b) Enzymatic
oxidation of glucose by GOx; (c) Enzymatically-triggered self-assembly of
peptides through proton gradient generation from a non-conductive surface
onto which is adsorbed GOx.
the Fmoc-AA-OH solution did not lead to any significant changes
of the normalized frequency shift (Figure 1c). These control
experiments highlight the crucial role of the enzymatic activity of
GOx in the multilayer film to direct the localized self-assembly
process of Fmoc-AA-OH through the generation of protons. To
increase the enzymatic proton production, several layers of GOx
alternated with PAH have been incorporated in the multilayer to
In solution, upside down vial tests of Fmoc-AA-OH (3.6
mg/mL) at different pH confirmed that gelation occurs in a few
minutes at pH ≤ 4 (Figure S1). We have ensured that Fmoc-AA-
OH (3.6 mg/mL, pH 5) can effectively lead to hydrogel formation
within roughly 10 min in the presence of GOx (6.25 µM) and
glucose (2 mg/mL, 11.10 mM) (Figure 1a). The isoelectric point
2
n n
obtain a PEI/(PSS/PAH) /(GOx/PAH) , film named (GOx/PAH) ,
with n = 2, 3 and 6. When a Fmoc-AA-OH/glucose solution was
put in contact with each of these films, a higher decrease of the
normalized frequency shift was observed in comparison to
(
IP) of GOx is around 4.2. It can thus be electrostatically
(GOx/PAH) film, indicating more deposited mass (Figure S5 in
1
adsorbed onto a positively charged surface at pH 7. To
immobilize GOx on a surface, we used the layer-by-layer
technique based on the alternated deposition of polyanions and
polycations on a surface,[16] a strategy already reported to
design bioreactors.[17] We first modified the surface by dipping it
into a solution of poly(ethylene imine) (PEI) and successively in
poly(styrene sulfonate) (PSS) and poly(allylamine hydrochloride)
ESI). After 40 minutes of contact, the thickness reached about ~
1.1 µm, ~ 2.3 µm, ~ 3.2 µm and ~ 3.3 µm for self-assemblies
induced by (GOx/PAH)1, (GOx/PAH)2, (GOx/PAH)3 and
(GOx/PAH)6 films respectively (Figure 2a). These thicknesses
were obtained from the QCM data by using the Voinova model
(See ESI part 3). Thus, the thickness of the self-assembled
hydrogel increases with the number of GOx/PAH layers and
levels off for n>3. This is probably due to the limited diffusion of
glucose into the multilayer for films exceeding 3 bilayers of
GOx/PAH on the top.
Because glucose is the provider of protons through its
oxidation by GOx., the influence of its concentration on the self-
assembly buildup has also been investigated. In addition to the 2
mg/mL concentration used up to now, we also studied the self-
assembly process and gelation that occur in presence of 0.5, 1,
1.5, 3, 4 and 5 mg/mL of glucose, keeping a constant
concentration of Fmoc-AA-OH (1 mg/mL). When brought in
contact with a (GOx/PAH)3 multilayer film, QCM-D monitoring
(
PAH) solutions to obtain a PEI/(PSS/PAH)
film. GOx was then deposited and capped by a PAH layer to
obtain the film PEI/(PSS/PAH) /(GOx/PAH) named
GOx/PAH) film. Its buildup was followed by QCM-D (Figure S2)
2
precursor multilayer
2
1
,
(
1
and its thickness was evaluated to ~8 nm (ESI, Part 3). Its
enzymatic activity was confirmed by spectrophotometric tests
(
Figure S3).
When a (GOx/PAH)
1
film was put in contact with a Fmoc-
AA-OH/glucose solution under a flow rate of 500 µL/min, an
important decrease of the normalized frequency shift was
observed by QCM-D over time indicating a deposition of mass
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Angewandte Chemie International Edition
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COMMUNICATION
shows no significant decrease of the frequency shift for
concentrations lower than 2 mg.mL, i.e. 0.5, 1 and 1.5 mg/mL,
despite the presence of few fibres as observed by SEM (Figures
S7a-c).
observes a steady increase of the intensity of these bands over
time during at least 12 hours confirming the gradual buildup of
the self-assembled layer. When GOx is replaced by BSA in the
multilayer, no formation of Fmoc-AA-OH hydrogel is observed by
ATR-FTIR (Figure S8).
The morphology of the Fmoc-AA-OH self-assembly,
obtained from (GOx/PAH) films (n=1,3) after 40 min of contact
n
with Fmoc-AA-OH/glucose solution was imaged by AFM in
contact mode in dry state and by SEM. A network of long fibres
extending up to several hundred nanometres was observed that
underpin the hydrogel structure (Figure S9). This fibrous network
a. 3
.5
.0
.5
.0
.5
.0
.5
.0
b. 0.030
0.025
3
2
2
1
1
0
0
0.020
0.015
0.010
0.005
0.000
is denser than the one obtained from (GOx/PAH)
2c and S10). To visualize the internal morphology of the
localized self-assembly, a (GOx/PAH) functionalized glass
1
film (Figures
n=1 n=2 n=3 n=6
GOx/PAH)
1
750
1700
1650
1600
-1
1550
(
n
Wavenumber (cm )
Wavenumber (cm )
-1
3
c.
d.
surface was put into contact with a Fmoc-AA-OH/glucose
solution for 16 h, rinsed and imaged by cryo-SEM. The cross-
section image shows the presence of an architecture of ~ 6 µm
in thickness all along the glass surface (Figure 2d) highlighting
the full covering of the substrate by the self-assembled hydrogel
and showing a regular thickness all along the surface (Figure
S11). It can be pointed that QCM and cryo-MEB indicate layer
thicknesses exceeding several micrometers even if the absolute
values differ by a factor of two. This may be due to the use of
the model to treat the QCM data. We also verified that when a
~
6 µm
~ 6 µm
Figure 2. (a) Thickness values of Fmoc-AA-OH self-assembly formed on
GOx/PAH) (GOx/PAH) (GOx/PAH) and (GOx/PAH) films. Standard
deviations are calculated from three independent experiments; (b) ATR-FTIR
spectra of (GOx/PAH) film in contact with Fmoc-AA-OH/glucose solution after
min (pink), 40 min (dashed blue), 1h (dashed dot dotted brown) and 12h
dotted red). These bands are visualized after subtraction of the spectra of
(
1
,
2
,
3
6
3
5
(
3
GOx/PAH) film is adsorbed on a specific area of the glass and
(
(
this substrate is entirely brought in contact with glucose and
Fmoc-AA-OH mixture, the resulting hydrogel is formed strictly in
the area pre-coated by the multilayer film. Only some peptide
based fibres have spread over several micrometres at the
interface between the multilayer area and the naked glass
3
GOx/PAH) film (Figure S6); (c) Height and phase AFM images (5.5 x 5.5
2
µm ) of Fmoc-AA-OH self-assembly (contact mode, dry state, z-scale 84 nm);
(
d) Cryo-SEM cross-section image of Fmoc-AA-OH self-assembly in the z-
section.
(
Figure S12).
It must be noted that a slight flow (500 µL/min) of Fmoc-
This means that the self-assembly can occur at these low
concentrations of glucose but no gelation starts. In contrast, an
important and almost equivalent frequency shift is observed for
each of the 3 higher glucose concentrations investigated. It thus
appears that a critical concentration which lies between 1.5 and
AA-OH/glucose was necessary for the self-assembly process to
occur: only a low QCM signal was observed when the mixture
was in contact with (GOx/PAH)
This can be explained by the fact that GOx requires a supply in
to be effective, continuously brought by the flow of reactants.
3
film without flow (Figure 3b).
2
mg/mL is necessary to get the formation of a hydrogel layer on
O
2
the surface (Figure S7c). Higher glucose concentrations do not
lead to layers thicker than the ~3.2 µm obtained with 2 mg/mL.
In addition, we also observed that the diameter of the smaller
peptide fibres observed by SEM is roughly 55 nm whatever the
glucose concentration used (Figure S7d).
When Fmoc-AA-OH/glucose solution was degassed and
injected with a similar flow rate, no decrease of the fundamental
frequency shift was observed confirming this hypothesis (Figure
2
S13). In order to provide in situ the fuel, i.e. O , to the system
without flow of the reactants, a second enzyme, the horseradish
peroxidase (HRP), was added onto the multilayer film. This
In order to confirm the self-assembly of Fmoc-AA-OH,
ATR-FTIR experiments were performed during the contact of
Fmoc-AA-OH/glucose solution with (GOx/PAH) films built on a
3
ZnSe crystal. When bringing the peptide/glucose solution in
contact with the surface an increase in intensity of the amide I
band region over time was observed. In particular three vibration
bands at 1686, 1643 and 1620 cm-1 appear (Figure 2b). The
band at 1620 cm-1 confirms a β-sheet structure adopted by the
enzyme can transform H
by GOx, into O
2
O
2
, produced when glucose is reduced
(Figure 3a).[ With respect to its IP 8.8 the
19]
2
following
multilayer
has
been
investigated
PEI/(PSS/PAH)
2
/GOx/PAH/PSS/HRP. Unfortunately, when this
film was brought in contact with Fmoc-AA-OH and glucose, no
self-assembly was observed (Figure S14). The efficiency of this
system is sensitive to the spatial distance between the two
enzymes: optimal motor can be effectively designed when both
enzymes are spatially very close together.[ Thus HRP was
directly adsorbed onto GOx leading to the following multilayer
self-assembly of Fmoc-AA-OH. In addition, the presence of the
band at 1686 cm-1 allows the assignment of the antiparallel β-
20]
sheet conformation which is consistent with observations done
on others peptide-based supramolecular hydrogels.[18] The band
at 1643 cm-1 is characteristic of an amide band involved in
PEI/(PSS/PAH) /(GOx/HRP) named (GOx/HRP). When this film
2
[
14a]
was brought in contact with a Fmoc-AA-OH/glucose without flow,
a decrease of the normalized frequency shift was measured
showing the self-assembly of Fmoc-AA-OH (Figure 3b) which
was confirmed by ATR-FTIR and AFM experiments (Figures S15
and S16).
polyproline II (PPII) conformation.
The band located at 1586
cm and the peak area between 1750-1700 cm-1 can be
-1
attributed to COO- antisymmetric stretch and C=O stretching of
COOH of gluconic acid Fmoc-AA-OH respectively. One
This article is protected by copyright. All rights reserved.

Angewandte Chemie International Edition
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COMMUNICATION
4170-4198. (b) G. N. Pandian, H. Sugiyama, Bull. Chem. Soc. Jpn.
2
0
2016, 89, 843-868.
a.
b.
Fmoc-AA-OH
solution
0
Rinsing step
Rinsing step
[8]
[9]
E.K. Johnson, D.J. Adams, P.J. Cameron, J. Am. Chem. Soc. 2010,
132, 5130-5136.
(
Fuel)
H+
Glucose + O2
H O
+
2
2
-20
P.S. Kubiak, S. Awhida, C. Hotchen, W. Deng, B. Alston, T. O.
McDonald, D.J. Adams, P.J. Cameron, Chem. Commun. 2015, 51,
HRP
GOx
-40
1
0427-10430.
[10] Liu, E. Kim, R.V. Ulijn, W.E. Bentley, G.F. Payne, Adv. Funct. Mater.
011, 21, 1575-1580.
-60
Top of the Multilayer
2
0
50
100
150
200
[11] J. Raeburn, B. Alston, J. Kroeger, T.O. McDonald, J.R. Howse, P.J.
Cameron, D.J. Adams, Mater. Horizons 2014, 1, 241-246.
Time (min)
[
12] Y. Liu, J.L. Terrel, C.Y. Tsao, H.C. Wu, V. Javvaji, E. Kim, Y. Cheng, F.
Y. Wang, R.V. Ulijn, S.R. Raghavan, G.W. Rubloff, W.E. Bentley, G.F.
Payne, Adv. Funct. Mater. 2012, 22, 3004-3012.
Figure 3. (a) Enzymatically-triggered proton gradient generated from
GOx/HRP) film; (b) Evolution of the normalized frequency shift (QCM-D) over
time when (GOx/PAH) film (red dotted line) and (GOx/HRP) film (blue line)
(
1
3
[13] A.G.L. Olive, N.H. Abdullah, I. Ziemecka, E. Mendes, R. Eelkema, J.H.
are brought in contact with Fmoc-AA-OH/glucose without flow.
van Esch, Angew. Chem. 2014, 126, 4216-4220; Angew. Chem. Int. Ed.
2014, 53, 4132-4136.
In summary, despite recent developments of enzyme-
assisted self-assembly strategies no approach has been
reported involving enzyme-immobilized surfaces to create a flow
of ions at an interface to initiate a self-assembly process. Herein,
we present a first enzymatic system based on GOx to produce
protons which trigger the self-assembly of a Fmoc-AA-OH
[14] (a) X. Mu, K.M. Eckes, M.M. Nguyen, L.J. Suggs, P. Ren,
Biomacromolecules 2012, 13, 3562-3571;(b) V. Jayawarna, M. Ali, T.A.
Jowitt, A.F. Miller, A. Saiani, J.E. Gough, R.V. Ulijn, Adv. Mater. 2006,
18, 611-614; (c) D.J. Adams, L.M. Mullen, M. Berta, L. Chen, W.J. Frith,
Soft Matter 2010, 6, 1971-1980.
[15] W. Cheng, Y. Li, Sci. China-Phys. Mech. Astron. 2016, 59, 678711-
678716.
2
peptide network. It requires the presence of O in solution. We
[
16] G. Decher, Science 1997, 277, 1232-1237.
also show that the simultaneous presence of GOx and HRP on
top of the multilayer allows circumventing the outside supply of
O through a cascade of reactions. Using this strategy allows
2
17 (a) M. Onda, Y. Lvov, K. Ariga, T. Kunitake, Biotechnol. Bioeng. 1996,
51, 163-167; (b) M. Onda, Y. Lvov, K. Ariga, T. Kunitake, J.
Fermentation Bioeng. 1996, 82, 502-506; (c) S. Zhang, S. Demoustier-
Champagne, A. M. Jonas, Biomacromolecules 2015, 16, 2382-2393.
getting rid of conductive substrates to realize proton-gradient
induced self-assemblies and thus to generalize this type of self-
assembly to almost any king of substrate, whatever its nature
and geometry. Such multi-enzymatic systems localized on
surfaces lead to molecular motors that can tune (i) the self-
assembly process, (ii) its resulting function, (iii) its
sensitivity/responsivity to surrounding stimuli and finally (iv) its
evolution over space and time. This approach is still in its
infancy but represents an exciting perspective for further
research.

18 N. Yamada, K. Ariga, M. Naito, K. Matsubara, E. Koyama, J. Am. Chem.
Soc. 1998, 120, 12192-12199;
[
[
19] J. Hernandez-Ruiz, M.B. Arnao, A.N. Hiner, F. Garcia-Canovas, M.
Acosta, Biochem. J. 2001, 354, 107-114.
20] L. Xin, C. Zhou, Z. Yang, D. Liu, Small 2013, 9, 3088-3091.
Keywords: Surface Chemistry • Coating • Self-Assembly •
Nanostructures • Supramolecular chemistry
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Angewandte Chemie International Edition
10.1002/anie.201709029
COMMUNICATION
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COMMUNICATION
The power of enzymes: multilayer film including a
Jennifer
Léonardo Martinez Mendez, Xiyu
Mao, Déborah Wagner, Marc
Schmutz, Morgane Rabineau,
Rodon
Fores,
Miguel
Fmoc-AA-O
-
Fmoc-AA-OH
bi-enzyme reaction system establishes a protons
gradient going from the bottom to the top, leading
to the localized self-assembly of peptides that
Enzymes
containing
multilayer film
Glucose
H+
underpinned
a
supramolecular hydrogel. This
Philippe Lavalle, Pierre Schaaf*,
Fouzia Boulmedais and Loïc Jierry*
Supramolecular
hydrogel
approach constitutes an alternative to electrode
surface to induce pH sensitive self-assembly
processes.
Page No. – Page No.
Localized Supramolecular Peptide
Self-Assembly Directed by Enzyme-
Induced Proton-Gradients
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