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Novel adsorbents produced from β-lactoglobulin, a low-cost milk protein, have shown a high affinity to inorganic As(iii) and As(v).

The ongoing COVID-19 pandemic has revealed that developing effective therapeutics against viruses might be outpaced by emerging variants,1–5 waning immunity,6–9 vaccine skepticism/hesitancy,10–12 lack of resources,13–16 and the time needed to develop virus-specific therapeutics,17,18 emphasizing the importance of non-pharmaceutical interventions as the first line of defense against virus outbreaks and pandemics.19–23 However, fighting the spread of airborne viruses has proven extremely challenging,23–28 much more if this needs to be achieved on a global scale and in an environmentally-friendly manner.29,30 Here, we introduce an aerosol filter made of granular material based on whey protein nanofibrils and iron oxyhydroxides nanoparticles. The material is environmentally-friendly, biodegradable, and composed mainly of a dairy industry byproduct.31 It features remarkable filtration efficiencies between 95.91% and 99.99% for both enveloped and non-enveloped viruses, including SARS-CoV-2, the influenza A virus strain H1N1, enterovirus 71, bacteriophage Φ6, and bacteriophage MS2. The developed material is safe to handle and recycle, with a simple baking step sufficient to inactivate trapped viruses. The high filtration efficiency, virtually-zero environmental impact, and low cost of the material illuminate a viable role in fighting current and future pandemics on a global scale.

We introduce a green and efficient approach for removing per- and polyfluoroalkyl substances (PFASs) based on the beta-lactoglobulin amyloid fibril membrane. The membrane exhibits superior adsorption capability for long-chain PFASs. At low pH, the membrane efficiency improved significantly due to enhanced electrostatic interactions between positively charged fibrils and negatively charged PFASs. Furthermore, intermolecular adhesion force measurements confirm the hydrophobic-hydrophobic interaction at the nanoscale with PFOS and PFOA representing perfluoroalkyl sulfonic acids (PFSAs) and perfluoroalkyl carboxylic acids (PFCAs), respectively. For real PFAS-contaminated water from the Xiaoqing River basin and under single-step filtration mode, the membrane exhibits high efficiency for removing both high (>mu g L-1) and trace (ng L-1) levels of the compounds. To demonstrate the scalability and generality, a commercial amyloid-carbon-based hybrid membrane is applied for removal of a range of long-chain and short-chain PFASs as well as their replacement compounds, offering complete removal of PFASs with >= 4 perfluorinated carbon atoms in the molecular structure and a removal efficiency of low molecular weight PFBA (3 perfluorinated carbon atoms) exceeding 96%. Analysis of the sustainability footprint reveals the superiority of the amyloid-carbon hybrid membrane for PFAS removal. Altogether, these results demonstrate a high potential of amyloid fibril membrane technology for the sustainable removal of PFASs from water., Environmental Science: Water Research & Technology, 7 (10), ISSN:2053-1400, ISSN:2053-1419

Water scarcity and contamination by biological pollutants are global challenges that significantly affect public health. Reverse osmosis, nanofiltration and ultrafiltration technologies are very effective for the elimination of pathogens and most contaminants but associated with considerable capital and operating costs, high energy consumption and the use of chlorinated chemicals to suppress membrane fouling. Additionally, the pressure needed by these techniques may disrupt the pathogenic microbial cell membranes, causing the release of genetic material (fragments of DNA, RNA and plasmids) into the water. Here, we introduce the simultaneous removal of both bacteria and associated genetic material using amyloid hybrid membranes, via a combined adsorption and size exclusion mechanism. Amyloid hybrid membranes can remove upto and beyond 99% of the genetic material by adsorption, where amyloid fibrils act as the primary adsorbing material. When the same membranes are surface-modified using chitosan, the anti-biofouling performance of the membranes improved significantly, with a bacterial removal efficiency exceeding 6 log. © 2020 The Royal Society of Chemistry., Nanoscale Advances, 2 (10), ISSN:2516-0230

Nuclear medicine uses various radioactive compounds for the administration into patients to diagnose and treat diseases, which generates large amounts of radioactively contaminated water. Currently, radioactively contaminated hospital wastewater has to be stored until the contained radionuclides have sufficiently decayed because cost-effective and efficient removal technologies are not available. Similar considerations apply in the nuclear power industry, with, however, decay times of the radionuclides several orders of magnitude higher. Previously, we reported hybrid membranes composed of amyloid fibrils produced from cheap and readily available proteins and activated carbon, which efficiently removed heavy metal ions and radioactive compounds from water. Here, we show that these membranes are highly efficient in the adsorption & removal of diverse, clinically relevant radioactive compounds from hospital wastewater by single-step filtration. The radionuclides technetium (Tc-99m), iodine (I-123) and gallium (Ga-68) can be removed from water with efficiencies above 99.8% in one single step. We also demonstrate the purification of a real clinical wastewater sample from a Swiss hospital containing iodine (I-131) and lutetium (Lu-177). With the use of single-photon emission computed tomography (SPECT) and positron emission tomography (PET), we were able to visualize the accumulation of the radioactive compounds within the membrane and demonstrate its outstanding performance. By converting large volumes of radioactive wastewater into low volumes of solid radioactive waste, the present technology emerges as a possible game-changer in the treatment of nuclear wastewater., Environmental Science: Water Research & Technology, 6 (12), ISSN:2053-1400, ISSN:2053-1419

The tap water quality in Peru fails to meet the World Health Organization (WHO) drinking water standards; consequently, the local population in Peru has been exposed over the last few years to harmful arsenic levels through water consumption. A field study was conducted in Peru between 2019 and 2020 using granular adsorbers and hybrid membranes based on the technology using milk protein nanofibril–carbon hybrid materials previously introduced in the literature by us (S. Bolisetty and R. Mezzenga, Nat. Nanotechnol., 2016, 11, 365). The performance was analyzed across 28 households as well as 3 community-based water treatment plants in some of the Peruvian arsenic burdened regions, covering a range of groundwater arsenic concentrations between 11 μg L−1 and 1.1 mg L−1. Three different kinds of filtration units were installed including the combined granular media and hybrid membrane (type I), hybrid membrane alone (type II), and granular media (type III), to determine the effectiveness of different filtration setups for arsenic removal in different regions. The arsenic removal by household filtration units and community filtration units shows a removal efficiency exceeding 99% at various initial arsenic concentrations for a duration up to nine months. In addition, it is shown that an aqueous NaOH solution can be used to regenerate the adsorbent, extending its operational lifetime and the overall capacity for As removal. High purification efficiency, very low cost, safety, little to no energy requirement, possibility of regeneration and simplicity of operation make this technology suitable for arsenic removal from drinking water in a broad range of urban and rural areas., Environmental Science: Water Research & Technology, 7 (12), ISSN:2053-1400, ISSN:2053-1419

The billion tons of synthetic-polymer-based materials (i.e. plastics) produced yearly are a great challenge for humanity. Nature produces even more natural polymers, yet they are sustainable. Proteins are sequence-defined natural polymers that are constantly recycled when living systems feed. Digestion is the protein depolymerization into amino acids (the monomers) followed by their re-assembly into new proteins of arbitrarily different sequence and function. This breaks a common recycling paradigm where a material is recycled into itself. Organisms feed off of random protein mixtures that are "recycled" into new proteins whose identity depends on the cell's specific needs. In this study, mixtures of several peptides and/or proteins are depolymerized into their amino acid constituents, and these amino acids are used to synthesize new fluorescent, and bioactive proteins extracellularly by using an amino-acid-free, cell-free transcription-translation (TX-TL) system. Specifically, three peptides (magainin II, glucagon, and somatostatin 28) are digested using thermolysin first and then using leucine aminopeptidase. The amino acids so produced are added to a commercial TX-TL system to produce fluorescent proteins. Furthermore, proteins with high relevance in materials engineering (beta-lactoglobulin films, used for water filtration, or silk fibroin solutions) are successfully recycled into biotechnologically relevant proteins (fluorescent proteins, catechol 2,3-dioxygenase)., Advanced Materials, 33 (44), ISSN:0935-9648, ISSN:1521-4095

Minimizing the spread of viruses in the environment is the first defense line when fighting outbreaks and pandemics, but the current SARS-CoV-2 pandemic demonstrates how difficult this is on global scale, particularly in a sustainable and environmental-friendly way. Here we introduce and develop a sustainable and bio-degradable anti-viral filtration membrane composed of amyloid nanofibrils made from food-grade milk proteins and iron oxyhydroxide nanoparticles synthesized in-situ from iron salts by simple pH-tuning. Thus, all the membrane components are made of environmentally friendly, non-toxic and widely available materials. The membrane has outstanding efficacy against a broad range of viruses, including enveloped, non-enveloped, airborne and waterborne viruses, such as SARS-CoV-2, H1N1 (the influenza A virus strain responsible for the swine flu pandemic in 2009), and enterovirus 71 (EV71; a non-enveloped virus resistant to harsh conditions such as highly acidic pH), highlighting a possible role in fighting the current and future viral outbreaks and pandemics., Nature Nanotechnology, 16, ISSN:1748-3387, ISSN:1748-3395

The billion tons of synthetic polymer-based materials (i.e. plastics) produced every year are one of the greatest challenges that humanity has to face. Nature produces even more natural polymers, yet they are sustainable. For example, proteins are sequence-defined natural polymers, that are constantly recycled when living systems feed. Indeed, digestion is the protein depolymerization into amino acids (i.e. the monomers) followed by their re-assembly into new proteins of arbitrarily different sequence and function. This process breaks a common recycling paradigm where a material is recycled into itself. Organisms feed of random protein mixtures that are ‘recycled’ into new proteins whose identity depends on the cell’s needs at the time of protein synthesis. Currently, advanced materials are increasingly made of proteins, but the abovementioned ideal recyclability of such materials has yet to be recognized and established. In this study mixtures of several (up to >30) peptides and/or proteins were depolymerized into their amino acid constituents, and these amino acids were used to synthesize new fluorescent, and bio-active proteins extra-cellularly by using an amino acid-free cell-free transcription-translation system. Proteins with high relevance in materials engineering (β-lactoglobulin films, used for water filtration, or silk fibroin solutions) were successfully recycled into biotechnologically relevant proteins (green, and red fluorescent proteins, catechol 2,3-dioxygenase). The potential long-term impact of this approach to recycling lies in its compatibility with circular-economy models where raw materials remain in use as long as possible, thus reducing the burden on the planet.

Processing information with conventional integrated circuits remains beset by the interconnect bottleneck: circuits made of smaller active devices need longer and narrower interconnects, which have become the prime source of power dissipation and clock rate saturation. Optical interchip communication provides a fast and energy-saving option that still misses a generic on-chip optical information processing by interconnect-free and reconfigurable Boolean arithmetic logic units (ALU). Considering metal plasmons as a platform with dual optical and electronic compatibilities, we forge interconnect-free, ultracompact plasmonic Boolean logic gates and reconfigure them, at will, into computing ALU without any redesign nor cascaded circuitry. We tailor the plasmon mode landscape of a single 2.6 μm

The efficient removal of the long-lived fission product 137Cs from radioactive water by a filter material based on whey protein fibrils and activated carbon.

We report a new strategy for efficient removal of F- from contaminated water streams, and it relies on carbon hybrid membranes made of amyloid fibril/ZrO2 nanoparticles (

Amyloid fibrils have evolved from purely pathological materials implicated in neurodegenerative diseases to efficient templates for last-generation functional materials and nanotechnologies. Due to their high intrinsic stiffness and extreme aspect ratio, amyloid fibril hydrogels can serve as ideal building blocks for material design and synthesis. Yet, in these gels, stiffness is generally not paired by toughness, and their fragile nature hinders significantly their widespread application. Here we introduce an amyloid-assisted biosilicification process, which leads to the formation of silicified nanofibrils (fibril–silica core–shell nanofilaments) with stiffness up to and beyond [Formula: see text] 20 GPa, approaching the Young’s moduli of many metal alloys and inorganic materials. The silica shell endows the silicified fibrils with large bending rigidity, reflected in hydrogels with elasticity three orders of magnitude beyond conventional amyloid fibril hydrogels. A constitutive theoretical model is proposed that, despite its simplicity, quantitatively interprets the nonmonotonic dependence of the gel elasticity upon the filaments bundling promoted by shear stresses. The application of these hybrid silica–amyloid hydrogels is demonstrated on the fabrication of mechanically stable aerogels generated via sequential solvent exchange, supercritical [Formula: see text] removal, and calcination of the amyloid core, leading to aerogels of specific surface area as high as 993 [Formula: see text] /g, among the highest values ever reported for aerogels. We finally show that the scope of amyloid hydrogels can be expanded considerably by generating double networks of amyloid and hydrophilic polymers, which combine excellent stiffness and toughness beyond those of each of the constitutive individual networks.

Water pollution is a global problem threatening the entire biosphere and affecting the life of many millions of people around the world. Not only is water pollution one of the foremost global risk factors for illness, diseases and death, but it also contributes to the continuous reduction of the available drinkable water worldwide. Delivering valuable solutions, which are easy to implement and affordable, often remains a challenge. Here we review the current state-of-the-art of available technologies for water purification and discuss their field of application for heavy metal ion removal, as heavy metal ions are the most harmful and widespread contaminants. We consider each technology in the context of sustainability, a largely neglected key factor, which may actually play a pivotal role in the implementation of each technology in real applications, and we introduce a compact index, the Ranking Efficiency Product (REP), to evaluate the efficiency and ease of implementation of the various technologies in this broader perspective. Emerging technologies, for which a detailed quantitative analysis and assessment is not yet possible according to this methodology, either due to scarcity or inhomogeneity of data, are discussed in the final part of the manuscript.

We present the optimization of experimental conditions to yield long, rigid apoferritin protein amyloid fibrils, as well as the corresponding fibrillation pathway. Fibril growth kinetics was followed using atomic force microscopy (AFM), transmission electron microscopy (TEM), dynamic light scattering (DLS), circular dichroism (CD), fourier-transform infrared spectroscopy (FTIR), and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Among the morphologies identified, we show that the conditions result in small aggregates, as well as medium and long fibrils. Extended incubation times led to progressive unfolding and hydrolysis of the proteins into very short peptide fragments. AFM, SDS-PAGE, and CD support a universal common fibrillation mechanism in which hydrolyzed fragments play the central role. These collective results provide convincing evidence that protein unfolding and complete hydrolysis of the proteins into very short peptide sequences are essential for the formation of the final apoferritin amyloid-like fibrils., Junta de Andalucia P11-FQM-8136 P18-RT-1373, Ministry of Science and Innovation, Spain (MICINN), Instituto de Salud Carlos III, Spanish Government PID2019-111461GB-I00, Boehringer Ingelheim

International audience; Processing information with conventional integrated circuits remains beset by the interconnect bottleneck: circuits made of smaller active devices need longer and narrower interconnects, which have become the prime source of power dissipation and clock rate saturation. Optical interchip communication provides a fast and energy-saving option that still misses a generic on-chip optical information processing by interconnect-free and reconfigurable Boolean arithmetic logic units (ALU). Considering metal plasmons as a platform with dual optical and electronic compatibilities, we forge interconnect-free, ultracompact plasmonic Boolean logic gates and reconfigure them, at will, into computing ALU without any redesign nor cascaded circuitry. We tailor the plasmon mode landscape of a single 2.6 μm2 planar gold cavity and demonstrate the operation and facile reconfiguration of all 2-input logic gates. The potential for higher complexity of the same logic unit is shown by a multi-input excitation and a phase control to realize an arithmetic 2-bit adder.

Amyloid fibrils have garnered increasing attention as viable building blocks for functional material design and synthesis, especially those derived from food and agricultural wastes. Here, amyloid fibrils generated from β-lactoglobulin, a by-product from cheese industries, have been successfully used as a template for the design of a new class of high-performance conductive aerogels with sensing properties. These mechanically stable aerogels with three-dimensional porous architecture have a large surface area (≈159 m2 g-1), low density (≈0.044 g cm-3), and high electrical conductivity (≈0.042 S cm-1). A pressure sensing device is developed from these aerogels based on their combined electrical conductivity and compressible properties. More interestingly, these aerogels can be employed to design novel enzyme sensors by exploiting the proteinaceous nature of amyloid fibrils. This study expands the scope of structured amyloid fibrils as scaffolds for in situ polymerization of conducting polymers, offering new opportunities to design materials with multiple functionalities.

International audience; In the context of the emerging field of quantum plasmonics, we demonstrate in this manuscript the wavelength-dependent propagation and sorting of single plasmons launched in a two-dimensional crystalline gold flake by a broadband quantum nanoemitter. The stream of single plasmons in the visible is produced by a nanodiamond hosting a single nitrogen-vacancy color center positioned in the near field of the mesoscopic metallic microplatelet. Spatially and spectrally resolved images of the single plasmon propagation in the pristine hexagonal flake, and then in the same structure after insertion of a Bragg mirror, are obtained by filtered image-plane acquisitions on a leakage-radiation microscope. Our work on two-dimensional crystalline structures paves the way to future fundamental studies and applications in quantum plasmonics.

Water contamination by organic pollutants is ubiquitous and hence a global concern due to detrimental effects on the environment and human health. Here, it is demonstrated that amyloid fibrils aerogels are ideal adsorbers for removing organic pollutants from water. To this end, amyloid fibrils prepared from β-lactoglobulin, the major constituent of milk whey protein, are used as building blocks for the fabrication of the aerogels. The adsorption of Bentazone, Bisphenol A, and Ibuprofen, as model pollutants, is evaluated under quasi-static conditions, without use of energy or pressure. Through adsorption by amyloid fibrils aerogel, excellent removal efficiencies of 92%, 78%, and 98% are demonstrated for Bentazone, Bisphenol A, and Ibuprofen, respectively. Furthermore, the maximum adsorption capacity of amyloid fibrils aerogel for Bentazone, Bisphenol A, and Ibuprofen is 54.2, 50.6, and 69.6 mg g-1 , respectively. To shed light on the adsorption equilibrium process, adsorption isotherms, binding constants, saturation limits, and the effect of pH are evaluated. Finally, the regeneration of the aerogel over three consecutive cycles is studied, exhibiting high reusability with no significant changes in its removal performance. These results point at amyloid fibrils aerogels as a sustainable, efficient, and inexpensive technology for alleviating the ubiquitous water contamination by organic pollutants.

This paper presents the extension of the classical torsional resonance viscometer towards the characterization of linear viscoelastic fluids. By simultaneously tracking multiple resonance frequencies, shear viscosity and elasticity can be monitored at multiple discrete frequencies at the same time. The proposed method is applied to the well-established sensor design of a simple rod-like structure, hence enabling a robust and versatile measurement system that can be used in different applications, such as in-line measurement or hand-held devices. In order to simultaneously control different resonance frequencies, multiple independent phase-locked loops are used, of which each subsystem is responsible for one natural vibration. An analytical description of the relationship between measurement parameters and physical fluid parameters is presented that is valid both for Newtonian and linear viscoelastic fluids. Consequently, calibration of the sensor is possible using Newtonian fluids only. To demonstrate the sensor, viscoelastic polymer and surfactant solutions are investigated at five frequencies between 2 kHz and 20 kHz. Additionally, the test fluids are characterized by means of a classical rotational rheometer (low frequency range) and diffusing-wave spectroscopy (high frequency range). The comparison of all methods shows very good agreement and validates the application of the sensor as resonant rheometer for viscoelastic fluids.

Hydrogen peroxide (H2O2) is an abundant molecule associated with biological functions and reacts with natural enzymes, such as catalase. Even though direct H2O2 measurement can be used to diagnose pathological conditions, such as infection and inflammation, H2O2 quantification further enables the detection of disease biomarkers in enzyme-linked assays (e.g., ELISA) in which enzymatic reactions may generate or consume H2O2. Such a quantification is often measured optically with organic dyes in biological media that suffer, however, from poor stability. Currently, the optical H2O2 biosensing without organic-dyes in biological media and at low, submicromolar, concentrations has yet to be achieved. Herein, we rationally design biomimetic artificial enzymes based on antioxidant CeO2 nanoparticles that become luminescent upon their Eu3+ doping. We vary systematically their diameter from 4 to 16 nm and study their catalase-mimetic antioxidant activity, manifested as catalytic H2O2 decomposition in aqueous soluti...

We show the purification of arsenic-contaminated water using amyloid fibril-based membranes, which adsorb both the arsenate (+5) and arsenite (+3) oxidation forms at efficiencies of ∼99%. Binding isotherms indicate that amyloid fibrils possess multiple binding residues capable of strongly adsorbing arsenic ions via metal-ligand interactions, delaying the saturation of the membrane. We also show that these membranes can be reused for several cycles without any efficiency drop, and validate our technology in purifying real contaminated ground water by removing arsenic with an efficiency as high as 99.6%. These results make this technology promising for inexpensive, efficient and low-energy removal of arsenic from contaminated water.

Amyloid-carbon hybrid membranes have exceptional performance in removing heavy metal ions from water because of the presence of multiple binding sites on the amyloid fibrils, but the binding process is still not fully understood. To understand the mechanisms of amyloid-metal ion binding, we perform adsorption isotherms on a model system given by β-lactoglobulin amyloid fibrils and four representative heavy metal ions: chromium (Cr), nickel (Ni), silver (Ag), and platinum (Pt). Furthermore, to get a comprehensive thermodynamic picture of the binding process between amino acid residues and heavy metals, we here use isothermal titration calorimetry on native β-lactoglobulin monomers and amyloid fibrils exposed to the two model metal ions, that is, silver and chromium. A conclusive thermodynamic insight on the binding process emerges by direct measurements of enthalpy and entropy changes, association binding constant, and average number of binding sites of the protein monomer and amyloid fibril. As a result of the strong amyloid binding affinity between amino acids and metal ions, when the protein is converted into amyloid fibrils and assembled into membranes, the resulting amyloid-activated carbon hybrids remove all the tested heavy metals with efficiencies beyond 99%. Importantly, the efficiency remains stable during several consecutive cycles, demonstrating a high adsorption capacity and a long lifetime and reusability of the membranes. The recovery of adsorbed precious metal ions converted into elemental metals is shown to be a general feature of these membranes, with platinum and silver successfully recovered from saturated hybrid membranes by a simple thermal reduction. The separation performance, evaluated on real electroplating industrial wastewater containing chromium and nickel, is found to exceed 99% at a permeability as high as 2.92 × 10

Industrial development, energy production and mining have led to dramatically increased levels of environmental pollutants such as heavy metal ions, metal cyanides and nuclear waste. Current technologies for purifying contaminated waters are typically expensive and ion specific, and there is therefore a significant need for new approaches. Here, we report inexpensive hybrid membranes made from protein amyloid fibrils and activated porous carbon that can be used to remove heavy metal ions and radioactive waste from water. During filtration, the concentration of heavy metal ions drops by three to five orders of magnitude per passage and the process can be repeated numerous times. Notably, their efficiency remains unaltered when filtering several ions simultaneously. The performance of the membrane is enabled by the ability of the amyloids to selectively absorb heavy metal pollutants from solutions. We also show that our membranes can be used to recycle valuable heavy metal contaminants by thermally reducing ions trapped in saturated membranes, leading to the creation of elemental metal nanoparticles and films.

Native silk fibroin (NSF) is a unique biomaterial with extraordinary mechanical and biochemical properties. These key characteristics are directly associated with the physical transformation of unstructured, soluble NSF into highly organized nano‐ and microscale fibrils rich in β‐sheet content. Here, it is shown that this NSF fibrillation process is accompanied by the development of intrinsic fluorescence in the visible range, upon near‐UV excitation, a phenomenon that has not been investigated in detail to date. Here, the optical and fluorescence characteristics of NSF fibrils are probed and a route for potential applications in the field of self‐assembled optically active biomaterials and systems is explored. In particular, it is demonstrated that NSF can be structured into autofluorescent microcapsules with a controllable level of β‐sheet content and fluorescence properties. Furthermore, a facile and efficient fabrication route that permits arbitrary patterns of NSF microcapsules to be deposited on substrates under ambient conditions is shown. The resulting fluorescent NSF patterns display a high level of photostability. These results demonstrate the potential of using native silk as a new class of biocompatible photonic material., Macromolecular Bioscience, 18 (4), ISSN:1616-5187, ISSN:1616-5195

Physical Review Letters, 120 (15), ISSN:0031-9007, ISSN:1079-7114

Self-assembly of the naturally occurring sweetening agent, glycyrrhizic acid (GA) in water is studied by small-angle X-ray scattering and microscopic techniques. Statistical analysis on atomic force microscopy images reveals the formation of ultralong GA fibrils with uniform thickness of 2.5 nm and right-handed twist with a pitch of 9 nm, independently of GA concentration. Transparent nematic GA hydrogels are exploited to create functional hybrid materials. Two-fold and three-fold hybrids are developed by introducing graphene oxide (GO) and in situ-synthesized gold nanoparticles (Au NPs) in the hydrogel matrix for catalysis applications. In the presence of GO, the catalytic efficiency of Au NPs in the reduction of p-nitrophenol to p-aminophenol is enhanced by 2.5 times. Gold microplate single crystals are further synthesized in the GA hydrogel, expanding the scope of these hybrids and demonstrating their versatility in materials design.

We characterized the sol–gel transition of positively charged fibrils composed of the model amphiphilic peptide RADARADARADARADA (RADA 16-I) using a combination of microscopy, light scattering, microrheology and rheology techniques, and we investigated the dependence of the hydrogel formation on fibril concentration and ionic strength. The peptide is initially present as a dispersion of short rigid fibrils with average length of about 100 nm. During incubation, the fibrils aggregate irreversibly into longer fibrils and fibrillar aggregates. At peptide concentrations in the range 3–6.5 g/L, the fibrillar aggregates form a weak gel network which can be destroyed upon dilution. Percolation occurs without the formation of a nematic phase at a critical peptide concentration which decreases with increasing ionic strength. The gel structure can be well described in the frame of the fractal gel theory considering the network as a collection of fibrillar aggregates characterized by self-similar structure with a fractal dimension of 1.34.

International audience; On-chip optoelectronic and all-optical information processing paradigms require compact implementation of signal transfer for which nanoscale surface plasmons circuitry offers relevant solutions. This work demonstrates the directional signal transmittance mediated by 2D plasmonic eigenmodes supported by crystalline cavities. Channel devices comprising two mesoscopic triangular input and output ports and sustaining delocalized, higher-order plasmon resonances in the visible to infra-red range are shown to enable the controllable transmittance between two confined entry and exit ports coupled over a distance exceeding 2 μm. The transmittance is attenuated by > 20dB upon rotating the incident linear polarization, thus offering a convenient switching mechanism. The optimal transmittance for a given operating wavelength depends on the geometrical design of the device that sets the spatial and spectral characteristic of the supporting delocalized mode. Our approach is highly versatile and opens the way to more complex information processing using pure plasmonic or hybrid nanophotonic architectures.

The programmable assembly of functional nanomaterials has been extensively addressed; however, their selective reversible assembly in response to an external stimulus has been more difficult to realize. The specificity and programmable interactions of DNA have been exploited for the rational self-assembly of DNA-conjugated nanoparticles, and here we demonstrate the sequence-controlled disaggregation of DNA-modified gold nanoparticles simply by employing two complementary oligonucleotides. Target oligonucleotides with perfectly matching sequence enabled dissociation of aggregated nanoparticles, whereas oligonucleotides differing by one nucleotide did not cause disassembly of the aggregated nanoparticles. Physical aspects of this process were characterized by UV-vis absorption, light scattering, and transmission electron microscopy. This strategy for programmed disassembly of gold nanoparticles in response to biological stimuli demonstrates a fundamentally important concept anticipated to be useful for diverse applications involving molecular recognition.

External magnetic field is a powerful approach to induce orientational order in originally disordered suspensions of magneto-responsive anisotropic particles. By small angle neutron scattering and optical birefringence measurement technology, we investigated the effect of magnetic field on the spatial ordering of hybrid amyloid fibrils with different aspect ratios (length-to-diameter) and flexibilities decorated by spherical Fe3O4 nanoparticles. A continuous paranematic ordering from an initially isotropic suspension was observed upon increasing magnetic field strength, with spatial orientation increasing with colloidal volume fraction. At constant dimensionless concentration, stiff hybrid fibrils with varying aspect ratios and volume fractions, fall on the same master curve, with equivalent degrees of ordering at identical magnetic fields. However, the semiflexible hybrid fibrils with contour length close to persistence length exhibit a lower degree of alignment. This is consistent with Khokhlov-Semenov theoretical predictions. These findings sharpen the experimental toolbox to design colloidal systems with controllable degree of orientational ordering.

Amyloid fibrils are charged semiflexible assemblies with very large aspect ratio (length to diameter, L/D). Because of this large aspect ratio, the isotropic (I) and nematic (N) phase coexistence expected from the first-order thermodynamic nature of the I-N phase transition, as predicted from the Onsager's theory, is vanishingly small and, in practice, challenging to experimentally observe. In this study we present a remarkable widening of the I + N biphasic region in β-lactoglobulin fibrils suspension via freeze-thaw (F-T) cycling. The demixing behavior can be induced and controlled by a slow growth of propagation front of the ice crystals, which grow by excluding the amyloid fibrils from the crystal phase and thus concentrating them in the liquid phase. The growth of the ice crystals is accompanied by the formation of concentrated and elongated tactoid-like structure in the liquid phase. During the subsequent thawing cycling, at large tactoid domains, the mismatch in density caused by the presence of amyloid fibrils is sufficient to generate a sedimentation of the N phase at the bottom of the vial, coexisting with an I phase on the top. We reason why, despite the remarkable stability of the coexisting I and N phases observed over several weeks after F-T cycling, the biphasic region is understood to be a nonequilibrium, metastable state. Yet, the results in this study suggest that the F-T treatment is an effective approach to stabilize multiphase coexistence of liquid crystalline phases in colloidal suspensions of anisotropic particles without the need of additives, such as depleting agents, needed to modify interaction potentials.

Protein nanofibrils were first discovered in the context of misfolding and neurodegenerative diseases but have recently been found in naturally occurring functional materials including algal adhesives, bacterial coatings, and even mammalian melanosomes. These physiologically beneficial roles have led to the exploration of their use as the basis for artificial protein-based functional materials for a range of applications as bioscaffolds and carrier agents. In this work, we fabricate core shell protein microgels stabilized by protein fibrillation with hierarchical structuring on scales ranging from a few nanometers to tens of microns. With the aid of droplet microfluidics, we exploit fibrillar protein self-assembly together with the aqueous phase separation of a polysaccharide and polyethylene glycol to control the internal structure of the microgels on the micro- and nanoscales. We further elucidate the local composition, morphology, and structural characteristics of the microgels and demonstrate a potential application of core shell protein microgels for controlling the storage and sequential release of small drug-like molecules. The controlled self-assembly of protein nanofibrils into hierarchical structures can be used in this manner to generate a class of nanomaterials with a range of potential functions and applications.

A unique procedure is developed to capture carbon nanotubes into closed virus-like protein cages with a controllable shell. The cross-linked shell varies in thickness within ≈10(0) -10(2) nm, and can be entirely removed by enzyme degradation. The cytotoxicity is entirely suppressed, but can be promoted again by enzymes and near-infrared light. These hybrids can be decorated with functional inorganic nanoparticles or processed into nanocomposites.

We study the fibrillation pathway of ovalbumin protein and report the simultaneous formation of several types of fibrils, with clear structural and physical differences. We compare the fibrillation mechanisms at low pH with and without salt, and follow the kinetics of fibrils growth by atomic force microscopy (AFM), static and dynamic light scattering (SLS, DLS), and small-angle X-ray scattering (SAXS). We show that, among the morphologies identified, long semiflexible amyloid fibrils (type I), with persistence length Lp∼3 μm, Young's modulus E∼2.8 GPa, and cross-β structure are formed. We also observe much more flexible fibrils (type III, Lp∼63 nm), that can assemble into multistranded ribbons with time. They show significantly lower intrinsic stiffness (1.1 GPa) and a secondary structure, which is not characteristic of the well-ordered amyloids, as determined by circular dichroism (CD), wide-angle X-ray scattering (WAXS), and attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR). In between these two main classes of fibrils, a third family, with intermediate flexibility (type II, Lp∼300 nm), is also resolved.

We have investigated the thermodynamic and dynamic behavior of multistranded β-lactoglobulin protein fibrils in water, by combining static, dynamic, and depolarized dynamic light scattering (SLS, DLS, DDLS), small angle neutron scattering (SANS), rheology, and cryogenic transmission electron microscopy (cryo-TEM). We focus on the region of the phase diagram at which ionic strength and concentration changes induce transitions in gelation and lyotropic liquid crystalline behavior. An increase in ionic strength, induced by NaCl salt, progressively causes the phase transitions from nematic (N) to gel (G) phases; a further increase causes the transition to a translucent phase and to a macroscopic phase separation, respectively. An increase in fibril concentration induces first a phase transition from an isotropic (I) to a nematic phase (N); a further increase induces the formation of a gel phase. The protein gel strength is investigated by rheology measurements. SANS and osmotic compressibility calculated by SLS measurements clearly capture the main features of the IN transition of β-lactoglobulin protein fibrils. The form and structure factors measured by scattering experiments are analyzed by the polymer reference interaction site model (PRISM). Dynamics of the protein fibrils at different concentrations, measured by polarized and depolarized dynamic light scattering, show both individual and collective diffusion after the isotropic-nematic transition. Above this transition, cryo-TEM images further demonstrate the alignment of the protein fibrils, which is quantified by a 2D order parameter. This work discusses comprehensively, both experimentally and theoretically, the thermodynamics and dynamic features of β-lactoglobulin amyloid fibrils in a vast region of the concentration-ionic strength phase diagram.

Complex coacervation driven by associative electrostatic interactions was studied in mixtures of exfoliated sodium-montmorillonite (Na(+)-MMT) nanoplatelets and fish gelatin, at a specific mixing ratio and room temperature. Structural and viscoelastic properties of the coacervate phase were investigated as a function of pH by means of different complementary techniques. Independent of the technique used, the results consistently showed that there is an optimum pH value at which the coacervate phase shows the tightest structure with highest elasticity. The solid-like coacervates showed an obvious shear-thinning behavior and network fracture but immediately recovered back into their original elastic character upon removal of the shear strain. The nonlinear mechanical response characterized by single step stress relaxation experiments revealed the same trend for the yield stress and isochronal shear modulus of the coacervates as a function of pH with a maximum at pH 3.0 and lower values at 2.5 and 3.5 pHs, followed by a very sharp drop at pH 4.0. Finally, small-angle X-ray scattering (SAXS) data confirmed that at pHs lower than 4.0 the coacervate phases were dense and structured with a characteristic length scale (ξ(SAXS)) of ~7-9 nm. Comparing the ξ(SAXS) with rheological characteristic length (ξ(rheol)) estimated from low-frequency linear viscoelastic data and network theory, it was concluded that both the strength of the electrostatic interactions and the conformation of the gelatin chains before and during of the coacervation process are responsible for the structure and rigidity of the coacervates.

This paper reports β-lactoglobulin amyloid protein fibrils directed synthesis of Titanium Dioxide (TiO2) hybrid nanowires. Protein fibrils act as templates to generate closely packed TiO2 nanoparticles on the surface of the fibrils using titanium (IV) bis (ammonium lactato) dihydroxide (TiBALDH) as precursor, resulting in the TiO2–coated amyloid hybrid nanowires. These amyloid fibrils also exhibit complexation with a luminescent water-soluble semiconductive polythiophene (P3HT). TiO2 nanowires behave as electron acceptor while, P3HT as electron donor. In this way, amyloid-TiO2 hybrid nanowires can serve in heterojunction photovoltaic devices. To demonstrate this, a photovoltaic active layer is prepared by spin coating the blended mixture of polythiophene-coated fibrils and amyloid-TiO2 hybrid nanowires. The current–voltage characteristics of these photovoltaic devices exhibit excellent fill factor of 0.53, photovoltaic current density of 3.97 mA·cm−2 and power conversion efficiency of 0.72%, highlighting a possible future role for amyloid-based templates in donor–acceptor devices, organic electronics and hybrid solar cells.

Amyloid fibrils are promising nanomaterials for technological applications such as biosensors, tissue engineering, drug delivery, and optoelectronics. Here we show that amyloid-metal nanoparticle hybrids can be used both as efficient active materials for wet catalysis and as membranes for continuous flow catalysis applications. Initially, amyloid fibrils generated in vitro from the nontoxic β-lactoglobulin protein act as templates for the synthesis of gold and palladium metal nanoparticles from salt precursors. The resulting hybrids possess catalytic features as demonstrated by evaluating their activity in a model catalytic reaction in water, e.g., the reduction of 4-nitrophenol into 4-aminophenol, with the rate constant of the reduction increasing with the concentration of amyloid-nanoparticle hybrids. Importantly, the same nanoparticles adsorbed onto fibrils surface show improved catalytic efficiency compared to the same unattached particles, pointing at the important role played by the amyloid fibril templates. Then, filter membranes are prepared from the metal nanoparticle-decorated amyloid fibrils by vacuum filtration. The resulting membranes serve as efficient flow catalysis active materials, with a complete catalytic conversion achieved within a single flow passage of a feeding solution through the membrane.

Fibrils of β-lactoglobulin, formed by heating at pH 2, were titrated with a sulfated polysaccharide (κ-carrageenan) to determine the morphology and mechanism of complex formation at low pH. Structural information on the resultant complexes was gathered using transmission electron microscopy, atomic force microscopy, Doppler electrophoresis, and small-angle neutron scattering. Electrophoresis demonstrated that the carrageenan complexed with protein fibrils until reaching a maximum complexation efficiency at a protein/polysaccharide (r) weight ratio of 5:3. Neutron scattering and microscopy indicated an increasing formation of spherical aggregates attached along the protein fibrils with increases in the carrageenan concentration. These globular particles had an average diameter of 30 nm. Small-angle neutron scattering of these complexes could be accurately described by a form factor corresponding to multistranded twisted ribbons with spherical aggregates along their contour length, arranged in a necklace configuration.

Amyloid fibrils resulting from uncontrolled peptide aggregation are associated with several neurodegenerative diseases. Their polymorphism depends on a number of factors including pH, ionic strength, electrostatic interactions, hydrophobic interactions, hydrogen bonding, aromatic stacking interactions, and chirality. Understanding the mechanism of amyloid fibril formation can improve strategies towards the prevention of fibrillation processes and enable a wide range of potential applications in nanotemplating and nanotechnology.