Water contamination is a global threat due to its damaging effects on the environment and human health. Water pollution by microplastics (MPs), dissolved natural organic matter (NOM), and other turbid particles is ubiquitous in water treatment. Here, we introduce lysozyme amyloid fibrils as a novel natural bio-flocculant and explore their ability to flocculate and precipitate the abovementioned undesired colloidal objects. Thanks to their positively charged surface in a very broad range of pH, lysozyme amyloid fibrils show an excellent turbidity removal efficiency of 98.2 and 97.9% for dispersed polystyrene MPs and humic acid (HA), respectively. Additionally, total organic carbon measurements confirm these results by exhibiting removal efficiencies of 93.4 and 61.9% for purifying water from dispersed MPs and dissolved HA, respectively. The comparison among amyloid fibrils, commercial flocculants (FeCl3 and polyaluminumchloride), and native lysozyme monomers points to the superiority of amyloid fibrils at the same dosage and sedimentation time. Furthermore, the turbidity of pristine and MP-spiked wastewater and lake water decreased after the treatment by amyloid fibrils, validating their coagulation-flocculation performance under natural conditions. All these results demonstrate lysozyme amyloid fibrils as an appropriate natural bio-flocculant for removing dispersed MPs, NOM, and turbid particles from water.
COVID-19 is primarily known as a respiratory disease caused by SARS-CoV-2. However, neurological symptoms such as memory loss, sensory confusion, severe headaches, and even stroke are reported in up to 30% of cases and can persist even after the infection is over (long COVID). These neurological symptoms are thought to be produced by the virus infecting the central nervous system, however we don't understand the molecular mechanisms triggering them. The neurological effects of COVID-19 share similarities to neurodegenerative diseases in which the presence of cytotoxic aggregated amyloid protein or peptides is a common feature. Following the hypothesis that some neurological symptoms of COVID-19 may also follow an amyloid etiology we identified two peptides from the SARS-CoV-2 proteome that self-assemble into amyloid assemblies. Furthermore, these amyloids were shown to be highly toxic to neuronal cells. We suggest that cytotoxic aggregates of SARS-CoV-2 proteins may trigger neurological symptoms in COVID-19.
Gelatin–graphene conductive biopolymer nanocomposites (CPCs) with ultralow percolation threshold are designed by reducing in situ graphene oxide nanosheets with ascorbic acid and suppressing the aggregation of the graphene nanosheets. The resulting conductive nanocomposites show a record-low electrical percolation threshold of 3.3 × 10−2 vol%, which arises from the homogeneous dispersion of the graphene nanosheets within the gelatin matrix. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
Outbreaks of waterborne viruses pose a massive threat to human health, claiming the lives of hundreds of thousands of people every year. Adsorption-based filtration offers a promising facile and environmentally friendly approach to help provide safe drinking water to a world population of almost 8 billion people, particularly in communities that lack the infrastructure for large-scale facilities. The search for a material that can effectively trap viruses has been mainly driven by a top-down approach, in which old and new materials have been tested for this purpose. Despite substantial advances, finding a material that achieves this crucial goal and meets all associated challenges remains elusive. We suggest that the road forward should strongly rely on a complementary bottom-up approach based on our fundamental understanding of virus interactions at interfaces. We review the state-of-the-art physicochemical knowledge of the forces that drive the adsorption of viruses at solid–water interfaces. Compared to other nanometric colloids, viruses have heterogeneous surface chemistry and diverse morphologies. We advocate that advancing our understanding of virus interactions would require describing their physicochemical properties using novel descriptors that reflect their heterogeneity and diversity. Several other related topics are also addressed, including the effect of coadsorbates on virus adsorption, virus inactivation at interfaces, and experimental considerations to ensure well-grounded research results. We finally conclude with selected examples of materials that made notable advances in the field.
The structure and functionality of foods are described from the perspective of recent advances in soft condensed matter physics. An overview is given of the structure and properties of food materials in terms of the physically relevant length scales. Recent developments in the understanding of the physics of gels, micelles, liquid crystals, biopolymer complexes and amorphous carbohydrates are presented.
Abstract Amyloids were long viewed as irreversible, pathological aggregates, often associated with neurodegenerative diseases 1 . However, recent insights challenge this view, providing evidence that reversible amyloids can form upon stress conditions and fulfil crucial cellular functions 2 . Yet, the molecular mechanisms regulating functional amyloids and the differences to their pathological counterparts remain poorly understood. Here we investigate the conserved principles of amyloid reversibility by studying the essential metabolic enzyme pyruvate kinase (PK) in yeast and human cells. We demonstrate that PK forms stress-dependent reversible amyloids through a pH-sensitive amyloid core. Stress- induced cytosolic acidification promotes aggregate formation via protonation of specific glutamate (in yeast) or histidine (in human) residues within the amyloid core. Our work thus unravels a conserved and potentially widespread mechanism underlying amyloid functionality and reversibility, fine-tuned to the respective physiological cellular pH range.
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