References of "Duwez, Anne-Sophie"
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See detailLinear and propeller-like fluoro-isoindigo based donor–acceptor small molecules for organic solar cells
Ouhib, Farid ULg; Tomassetti, Mirco ULg; Dierckx, Wauter et al

in Organic Electronics (2015), 20

Two donor–acceptor type fluoro-isoindigo based small molecule semiconductors are syn- thesized and their optical, electrochemical, thermal, and charge transport properties are investigated. The two ... [more ▼]

Two donor–acceptor type fluoro-isoindigo based small molecule semiconductors are syn- thesized and their optical, electrochemical, thermal, and charge transport properties are investigated. The two molecular chromophores differ by their architecture, linear (M1) vs propeller-like (M2). Both molecules present a broad absorption in the visible range and a low optical HOMO–LUMO gap (?1.6 eV). AFM images of solution-processed thin films show that the trigonal molecule M2 forms highly oriented fibrils after a few seconds of solvent vapor annealing. The materials are evaluated as electron donor components in bulk heterojunction organic solar cells using PC61BM as the electron acceptor. The devices based on the propeller-like molecule M2 exhibit a high open-circuit voltage (around 1.0 V) and a power conversion efficiency of 2.23%. [less ▲]

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See detailConformational properties of helical foldamers under force
Willet, Nicolas ULg; Hinterdorfer, Peter; Lecommandoux, Sébastien et al

Conference (2015, February)

The aim of this study is to investigate the mechanochemical behavior of foldamers able to change their conformation is a stimuli-responsive way. Peptidic secondary structures were studied in detail by ... [more ▼]

The aim of this study is to investigate the mechanochemical behavior of foldamers able to change their conformation is a stimuli-responsive way. Peptidic secondary structures were studied in detail by atomic force microscopy (AFM) at the single-molecule level. Synthetic copolymers containing a polypeptide block were prepared by N-carboxyanhydride amino acid ring-opening polymerization. The polymer chains were grafted onto gold surfaces and their mechanochemical behavior was then studied by AFM single-molecule force spectroscopy (SMFS). The investigated polypeptide blocks were based on polyglutamate, which undergoes transitions from alpha-helix to random coil. This can be induced by external stimuli (pH, ionic strength, temperature) or simply by applying a force. The mechanically driven unfolding of the helical foldamer was characterized in detail. Stretching the folded peptide resulted in original features in the force-distance traces. Plateaus that are specific for the helical conformation were detected, quantified and discussed. Pulling-relaxing SMFS experiments were performed and led to a better understanding of the mechanically induced unfolding of an alpha-helix as a reversible phenomenon. [less ▲]

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See detailSingle-Molecule Force Spectroscopy on Synthetic Helical Nanoarchitectures
Devaux, Floriane ULg; Duwez, Anne-Sophie ULg; Huc, Ivan et al

Poster (2015, February)

Foldamers are artificial folded molecular architectures inspired by the structures and functions of natural biopolymers. Folding is the process selected by nature to control the conformation of its ... [more ▼]

Foldamers are artificial folded molecular architectures inspired by the structures and functions of natural biopolymers. Folding is the process selected by nature to control the conformation of its molecular machinery to carry out chemical functions and mechanical tasks, such as en-zyme catalysis, duplication in nucleic acids, force generation,... During the last decade of research on foldamers [1], synthetic oligomers able to adopt well-defined and predictable folded conformations, such as helices, have been proposed. Recent progress has shown that stepwise chemical synthesis and molecular design based on aromatic oligoamide backbones enable to produce large helically folded molecular architectures. The shape and stiffness of the backbone, local conformational preferences, specific interactions between distant monomers in sequences, as well as the action of external parameters such as the solvent or the presence of ions, can be combine to induce folding tendency. A remarkable aspect of these architectures is that they can give rise to folded patterns that have no in natural counterparts biopolymer structures. For instance, helices whose diameter varies along the se-quence, helices possessing a handedness inversion centre, herringbone helices have been reported. The objective of the project is to synthesize various helical nanorchitectures based on an oli-goamide aromatic backbone and to obtain a detailed picture of their dynamical conformation in solution, as well as, their mechanochemical properties, by AFM-based single molecule force spectroscopy. It is worth mentioning that an important sub-objective of this project is to probe intramolecular interactions in small synthetic molecules with the AFM. Indeed, whereas single-molecule force spectroscopy on macromolecules (proteins and synthetic polymers) is widely exploited[2], implementing single-molecule force spectroscopy on small molecules, such as the foldamers proposed here, remains a major challenge[3]. [1] For a review, see G. Guichard and I. Huc, Chem. Commun. 2011, 47, 5933–5941. [2]E. M. Puchner, H. E.Gaub, Curr. Opin. Struct. Biol. 2009, 19, 605–614. [3]P. Lussis, A.-S. Duwez, Nature Nanotech. 2011, 6, 553-557 [less ▲]

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See detailInfluence of the protein context on the polyglutamine length-dependent elongation of amyloid fibrils
Huynen, Céline ULg; Willet, Nicolas ULg; Duwez, Anne-Sophie ULg et al

in Biochimica et Biophysica Acta-Proteins and Proteomics (2014)

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See detailPhysisorbed poly(ethylene oxide) is a robust tether for AFM-based single-molecule force spectroscopy
Willet, Nicolas ULg; Lussis, Perrine ULg; Giamblanco, Nicoletta et al

Conference (2014, December 01)

Atomic force microscopy (AFM)-based single-molecule force spectroscopy is a prevalent tool for the exploration of individual (bio)molecules, providing exquisite information on many molecular-level ... [more ▼]

Atomic force microscopy (AFM)-based single-molecule force spectroscopy is a prevalent tool for the exploration of individual (bio)molecules, providing exquisite information on many molecular-level processes. For example, proteins, DNA, polysaccharides, supramolecular polymers and polyelectrolytes have been investigated, revealing details about the strength of intramolecular interactions, folding and unfolding pathways, mechanics, conformational changes, reactivity, kinetics, etc. For each particular system under investigation, the experimental design is a decisive phase that often involves a multistep chemical protocol, including grafting, derivatization, coupling, (de-)protection, and other functionalization reactions. Procedures of sample preparation are often complex and time-consuming. Hence, there is a need for new general platforms allowing for straightforward sample preparation adapted to single-molecule studies, i.e. a tight attachment to both the substrate and the tip, and a low density to favor single-molecule detection. We report here on the use of poly(ethylene oxide) (PEO) as a tether to probe various properties of individual molecules. The polymeric linker acts as a handle that stably binds to the AFM tip. The simple adsorption of poly(ethylene oxide) to the tip is versatile and provides an appropriate system configuration for the investigation of many different biological and synthetic molecular systems. To attest for this versatility and adequacy with advanced single-molecule investigation, we present different examples of PEO-mediated studies about the unfolding of a synthetic peptide, the mechanochemical behavior of a molecular machine and finally the stability of a metallo-supramolecular complexed polymer. All the requirements for the study of peptide conformation, tiny molecular machines or metallo-supramolecular interactions in solution are here fulfilled. More generally, this method based on non-covalent sorption of PEO on an AFM tip, can be implemented in a wide range of solvents, for the study of many intra- or intermolecular phenomena at the single-molecule level over orders of magnitude of force loading rates. Connecting PEO tethers to a very broad variety of (bio)molecules is a facile and versatile route. The commercial availability of many different functional PEOs makes this tethering strategy even more accessible. [less ▲]

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See detailRole of the polyQ length and non-polyQ regions during the aggregation process into amyloid fibrils of model polyQ proteins
Huynen, Céline ULg; Willet, Nicolas ULg; Buell, Alexander K et al

Poster (2014, November 26)

Nine neurodegenerative disorders, referred to as polyglutamine diseases and including Huntington’s disease, are associated with the abnormal expansion of a polyglutamine tract inside nine unrelated ... [more ▼]

Nine neurodegenerative disorders, referred to as polyglutamine diseases and including Huntington’s disease, are associated with the abnormal expansion of a polyglutamine tract inside nine unrelated proteins. This polyQ expansion is thought to be the major determinant in the development of neurotoxicity, triggering protein aggregation into amyloid fibrils. A large body of evidence however suggests that non-polyQ regions modulate the aggregation process triggered by polyQ expansions. The interplay between the polyQ tract and non-polyQ regions is complex and still not fully understood. In order to better understand it, we previously designed and characterized model polyQ proteins made of the beta-lactamase BlaP with 23, 30, 55 and 79Q inserted at position 197 or 216. Our first results had indicated that our model is relevant to study polyQ aggregation since it recapitulates the aggregation properties of polyQ disease-associated proteins: there is a Q-threshold for the spontaneous formation of amyloid fibrils in solution, and above the threshold, the longer the polyQ, the faster the aggregation. Moreover, the structure of BlaP and the position of insertion of the polyQ tract influence their aggregation properties in solution. This work aims to better understand, at the molecular level, (i) the precise role of the polyQ length (23, 30, 55, 61, 67, 73 and 79Q), (ii) the conformation of the host protein (native or unfolded BlaP), (iii) the location of the polyQ tract within BlaP (197 or 216), (iv) the flexibility of the polyQ flanking sequences, and (v) the origin of constraints applied by BlaP to the inserted polyQ tract (at its N- or C-terminal end) on the structural, thermodynamic and aggregation properties of BlaP-polyQ chimeras, using a wide range of biophysical techniques (e.g., spectroscopy methods, quartz crystal microbalance, atomic force microscopy and dynamic light scattering). The effect on the aggregation properties will be determined on the spontaneous aggregation into amyloid fibrils in solution, and on the nucleation and on the elongation steps of amyloid fibril formation. For this purpose, new chimeras containing 61, 67 and 73Q at position 197, or 55Q inserted at position 197 in between two different protease’s cleavage sites, that are relatively flexible, will be moreover created. Our results first demonstrate that the spontaneous aggregation into amyloid fibrils in solution is correlated to the polyQ length with an exponential growth function, and that the elongation rate is linearly correlated to the polyQ length, independently of the protein context (i.e., conformation of BlaP, and/or location of the polyQ tract, and/or polyQ peptides inserted or not within BlaP). However, the location of the polyQ tract inside BlaP, and/or its conformational state, and/or the flexibility of polyQ flanking sequences, and/or the origin of constraints applied to the polyQ tract drastically influence the ability of a polyQ tract to trigger the nucleation and/or the elongation step of amyloid fibrils (variation in the Q-threshold and in the absolute rate of both steps). Altogether, our results suggest that non-polyQ regions constitute an additional potential therapeutic target, more specific than drugs targeting the polyQ sequence, to interfere with the nucleation and/or the elongation of amyloid fibrils, associated to neurotoxicity. A possible drug could be constituted by a ligand specific to non-polyQ regions of disease-associated proteins, which further increases the constraints applied to the polyQ expansion to prevent the disease onset and/or progression. [less ▲]

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See detailRole of non-polyQ regions on the aggregation process by polyQ proteins into amyloid fibrils
Huynen, Céline ULg; Willet, Nicolas ULg; Buell, Alexander K et al

Poster (2014, October 18)

Nine neurodegenerative disorders, referred to as polyglutamine diseases and including Huntington’s disease, are associated with the abnormal expansion of a polyglutamine tract inside nine unrelated ... [more ▼]

Nine neurodegenerative disorders, referred to as polyglutamine diseases and including Huntington’s disease, are associated with the abnormal expansion of a polyglutamine tract inside nine unrelated proteins. This polyQ expansion is thought to be the major determinant in the development of neurotoxicity, triggering protein aggregation into amyloid fibrils. A large body of evidence however indicates that non-polyQ regions modulate the aggregation process triggered by polyQ expansions. The interplay between the polyQ tract and non-polyQ regions is complex and still not fully understood. In order to better understand it, we previously designed and characterized model polyQ proteins made of the beta-lactamase BlaP and a 23, 30, 55 or 79Q tract inserted in position 197 or 216. These chimeras recapitulate the aggregation properties of polyQ disease-associated proteins: there is a Q-threshold for the formation of amyloid fibrils, and above the threshold, the longer the polyQ, the faster the aggregation. Moreover, the structure of BlaP (native or unfolded) and the position of insertion of the polyQ tract (197 versus 216) influence their aggregation properties. In this work, (i) we discuss the role of the conformation of the host protein, BlaP, and of the location of the polyQ within BlaP on the different phases of amyloid fibril formation, the nucleation and elongation steps, using mainly quartz crystal microbalance (QCM), atomic force microscopy (AFM). Our results highlight a linear dependence of the polyQ length on the elongation rate whatever the insertion site and the conformation of BlaP. These two parameters however drastically influence the ability of a polyQ tract to trigger the nucleation and the elongation steps of amyloid fibril formation. (ii) Finally, we investigate the precise aggregation threshold and the modulating role of the N- and C-terminal polyQ flanking sequences in position 197 of BlaP by creating and characterizing new chimeras containing intermediate length polyQ tracts in position 197, or polyQ tracts inserted between two cleavage sites in position 197, respectively. We observe that the propensity to trigger the full process of amyloid fibril formation and its rate seems to be largely dependent on the polyQ length and on the polyQ flanking sequences. Altogether our results contribute to identify the important species and elements (polyQ or non-polyQ regions, monomers, oligomers or fibrils) during the aggregation process into amyloid fibrils to interfere with the latter associated with neurotoxicity. [less ▲]

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See detailA facile and fast electrochemical route to produce functional few-layer graphene sheets for lithium battery anode application
Ouhib, Farid ULg; Aqil, Abdelhafid ULg; Thomassin, Jean-Michel ULg et al

in Journal of Materials Chemistry A (2014), 2(37), 15298-15302

A simple approach for the production of polymer functionalized graphene nanosheets is reported. The resulting polyacrylonitrile chemisorbed on graphene sheets is made of 1 to 2 layers, with a large ... [more ▼]

A simple approach for the production of polymer functionalized graphene nanosheets is reported. The resulting polyacrylonitrile chemisorbed on graphene sheets is made of 1 to 2 layers, with a large majority of graphene single-layers. This novel functionalized graphene exhibits good cycling stability as an anode in Li-ion batteries without a conductive additive or binder. [less ▲]

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See detailRole of non-polyQ regions on the aggregation process by polyQ proteins into amyloid fibrils
Huynen, Céline ULg; Willet, Nicolas ULg; Buell, Alexander K et al

Poster (2014, July 28)

Nine neurodegenerative disorders, referred to as polyglutamine diseases and including Huntington’s disease, are associated with the abnormal expansion of a polyglutamine tract inside nine unrelated ... [more ▼]

Nine neurodegenerative disorders, referred to as polyglutamine diseases and including Huntington’s disease, are associated with the abnormal expansion of a polyglutamine tract inside nine unrelated proteins. This polyQ expansion is thought to be the major determinant in the development of neurotoxicity, triggering protein aggregation into amyloid fibrils. A large body of evidence however indicates that non-polyQ regions modulate the aggregation process triggered by polyQ expansions. The interplay between the polyQ tract and non-polyQ regions is complex and still not fully understood. In order to better understand it, we previously designed and characterized model polyQ proteins made of the beta-lactamase BlaP and a 23, 30, 55 or 79Q tract inserted in position 197 or 216. These chimeras recapitulate the aggregation properties of polyQ disease-associated proteins: there is a Q threshold for the formation of amyloid fibrils, and above the threshold, the longer the polyQ, the faster the aggregation. Moreover, the structure of BlaP (native or unfolded) and the position of insertion of the polyQ tract (197 versus 216) influence their aggregation properties. In this work, (i) we will discuss the role of the conformation of the host protein, BlaP, and of the location of the polyQ within BlaP on the different phases of amyloid fibril formation, the nucleation and elongation steps, using mainly quartz crystal microbalance (QCM), atomic force microscopy (AFM) and dynamic light scattering (DLS); and (ii) we will investigate the precise aggregation threshold and the modulating role of the N- and C-terminal polyQ flanking sequences in position 197 of BlaP by creating and characterizing new chimeras containing intermediate length polyQ tracts in position 197, or polyQ tracts inserted between two cleavage sites in position 197, respectively. Our results highlight a linear dependence of the polyQ length on the elongation rate whatever the insertion site and the conformation of BlaP. These two parameters however drastically influence the ability of a polyQ tract to trigger the nucleation and the elongation steps of amyloid fibril formation. Finally, we observed that the propensity to form amyloid fibrils and its rate seems to be largely dependent on the polyQ length and on the polyQ flanking sequences. Altogether our results contribute to identify the important species and elements (polyQ or non-polyQ regions, monomers, oligomers or fibrils) during the aggregation process into amyloid fibrils to interfere with the latter associated with neurotoxicity. [less ▲]

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See detailCollapsing and reswelling kinetics of thermoresponsive polymers on surfaces: a matter of confinement and constraints
Willet, Nicolas ULg; Gabriel, Sabine ULg; Jérôme, Christine ULg et al

in Soft Matter (2014), 10

We report on the collapsing and reswelling ability of grafted poly(methyl vinyl ether) chains of different molecular architectures. In order to study the influence of constraints and confinement of the ... [more ▼]

We report on the collapsing and reswelling ability of grafted poly(methyl vinyl ether) chains of different molecular architectures. In order to study the influence of constraints and confinement of the chains, the polymer was grafted onto AFM tips, as a model of a curved nano-sized surface, and onto macroscopic silicon substrates for comparison purposes. AFM-based force spectroscopy experiments were performed to characterise at the nanoscale the temperature-dependent collapsing process and the reversibility to the swollen state on both substrates. The reversible character of the thermoresponsive transition and its kinetics were shown to greatly depend on the polymer architecture and the constraints encountered by the chains. [less ▲]

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See detailBiointerface multiparametric study of intraocular lens acrylic materials.
Bertrand, Virginie ULg; Bozukova, Dimitriya; Svaldo Lanero, Tiziana et al

in Journal of cataract and refractive surgery (2014), 40(9), 1536-44

PURPOSE: To compare hydrophilic and hydrophobic acrylic materials designed for intraocular lenses in a multiparametric investigation in a liquid environment to highlight their properties in terms of ... [more ▼]

PURPOSE: To compare hydrophilic and hydrophobic acrylic materials designed for intraocular lenses in a multiparametric investigation in a liquid environment to highlight their properties in terms of adhesion forces, lens epithelial cell (LEC) adhesion, and tissue response as indicators of the risk for posterior capsule opacification (PCO) development. SETTING: University of Liege, Liege, Belgium. DESIGN: Experimental study. METHODS: The hydrophobicity and surface adhesion force were assessed using contact-angle and atomic force microscopy measurements. The bioadhesiveness of the disks and the tissue response were determined by in vitro experiments using bovine serum albumin and porcine LECs and by in vivo rabbit subcutaneous implantation, respectively. RESULTS: Increasing surface hydrophobicity led to a greater surface-adhesion force and greater LEC adhesion. After 1 month, the rabbit subcutaneous implants showed a similar thin layer of fibrous capsule surrounding the disks without extensive inflammation. A layer of rounded cells in contact with disks was detected on the hydrophobic samples only. CONCLUSIONS: Hydrophobic acrylic disks that have been associated with a reduced risk for PCO in clinical studies showed increased tackiness. FINANCIAL DISCLOSURES: Proprietary or commercial disclosures are listed after the references. [less ▲]

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See detailRobust bio-inspired antibacterial surfaces based on the covalent binding of peptides on functional atmospheric plasma thin films
Mauchauffé, Rodolphe; Moreno-Couranjou, Maryline; Boscher, Nicolas D. et al

in Journal of Materials Chemistry B (2014), 2

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See detailProbing the mobility of catenane rings in single molecules
Van Quaethem, Anne; Lussis, Perrine; Leigh, David A. et al

in Chemical Science (2014), 5

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See detailIon Mobility Spectrometry Reveals Duplex DNA Dissociation Intermediates
Burmistrova, Anastasia; Gabelica, Valérie; Duwez, Anne-Sophie ULg et al

in Journal of the American Society for Mass Spectrometry (2013), 24

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See detailThe Dynamics of Complex Formation between Amylose Brushes on Gold and Fatty Acids by QCM‐D
Cao, Zheng; Tsoufis, Theodoros; Svaldo Lanero, Tiziana ULg et al

in Biomacromolecules (2013), 14

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See detailThe pulling force of a tiny synthetic molecular machine
Svaldo Lanero, Tiziana ULg; Duwez, Anne-Sophie ULg

in Europhysics News (2013), 44

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See detailSynthesis of poly(vinyl acetate)-b-poly(vinyl chloride) block copolymers by cobalt-mediated radical polymerization (CMRP)
Piette, Yasmine; Debuigne, Antoine ULg; Bodart, Vinent et al

in Polymer Chemistry (2013), 4(5), 1685-1693

The synthesis of poly(vinyl acetate)-b-poly(vinyl chloride) (PVAc-b-PVC) block copolymers by Cobalt-Mediated Radical Polymerization (CMRP) is investigated for the first time in this paper. A PVAc–Co(acac ... [more ▼]

The synthesis of poly(vinyl acetate)-b-poly(vinyl chloride) (PVAc-b-PVC) block copolymers by Cobalt-Mediated Radical Polymerization (CMRP) is investigated for the first time in this paper. A PVAc–Co(acac)2 macroinitiator is prepared by CMRP using the V-70/Co(acac)2 binary system or a preformed alkylcobalt(III) compound. Then, the block copolymerization occurs in the bulk at 40 °C by the addition of VC. The addition of water to the polymerization medium or the slow generation of alkyl radicals during the whole polymerization is beneficial to the process by consuming part of the excess of deactivator (Co(acac)2) that blocks the polymer chains into the dormant form. Dynamic light scattering (DLS) measurements and AFM analyses evidence that the PVAc-b-PVC forms core–shell micelles in a selective solvent of the PVAc block, i.e. methanol, evidencing the blocky structure of the copolymer. PVAc-b-P(VC-co-VAc) copolymers are also successfully prepared by initiating the radical copolymerization of VC and VAc at 40 °C from a PVAc–Co(acac)2 macroinitiator. [less ▲]

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See detailFunctional nanogels as platforms for imparting antibacterial, antibiofilm, and antiadhesion activities to stainless steel
Faure, Emilie ULg; Falentin, Céline ULg; Svaldo Lanero, Tiziana ULg et al

in Advanced Functional Materials (2012), 22(24), 5271-5282

In this work, long-term antibacterial, antiadhesion, and antibiofilm activities are afforded to industrial stainless steel surfaces following a green and bio-inspired strategy. Starting from catechol ... [more ▼]

In this work, long-term antibacterial, antiadhesion, and antibiofilm activities are afforded to industrial stainless steel surfaces following a green and bio-inspired strategy. Starting from catechol bearing synthetic polymers, the film cross-linking and the grafting of active (bio)molecules are possible under environmentally friendly conditions (in aqueous media and at room temperature). A bio-inspired polyelectrolyte, a polycation-bearing catechol, is used as the film-anchoring polymer while a poly(methacrylamide)-bearing quinone groups serves as the cross-linking agent in combination with a polymer bearing primary amine groups. The amine/quinone reaction is exploited to prepare stable solutions of nanogels in water at room temperature that can be easily deposited to stainless steel. This coating provides quinonefunctionalized surfaces that are then used to covalently anchor active (bio) molecules (antibiofi lm enzyme and antiadhesion polymer) through thiol/ quinone reactions. [less ▲]

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