Sustainable Removal of Microplastics and Natural Organic Matter from Water by Coagulation-Flocculation with Protein Amyloid Fibrils.

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.

Selective and Efficient Removal of Fluoride from Water: In Situ Engineered Amyloid Fibril/ZrO2 Hybrid Membranes.

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 (<10 nm). These membranes exhibit superior selectivity for F- against various competitive ions, with a distribution coefficient (Kd ) as high as 6820 mL g-1 , exceeding commercial ion-exchange resins (IRA-900) by 180 times and outdoing the performance of most commercial carbon-activated aluminum membranes. At both low and high (ca. 200 mg L-1 ) F- concentrations, the membrane efficiency exceeds 99.5 % removal. For real untreated municipal tap water (ca. 2.8 mg L-1 ) under continuous operating mode, data indicates that about 1750 kg water m-2 membrane can be treated while maintaining drinking water quality, and the saturated membranes can be regenerated and reused several times without decrease in performance. This technology is promising for mitigating the problem of fluoride water contamination worldwide.

Oil transfer converts phosphatidylcholine vesicles into nonlamellar lyotropic liquid crystalline particles.

There is a need for the development of low-energy dispersion methods tailored to the formation of phospholipid-based nonlamellar lyotropic liquid crystalline (LLC) particles for delivery system applications. Here, facile formation of nonlamellar LLC particles was obtained by simple mixing of a phosphatidylcholine (PC) liposome solution and an oil-in-water emulsion, with limonene or isooctane as an oil. The internal structure of the particles was controlled by the PC-to-oil ratio, consistently with the sequence observed in bulk phase. For the first time, reverse micellar cubosomes with Fm3̅m inner structure were produced. The size, morphology, and inner structure of the particles were characterized by small-angle X-ray scattering (SAXS), dynamic light scattering (DLS), and freeze-fracture cryo scanning electron microscopy (cryo-SEM). These findings pave the way to new strategies in low-energy formulation of LLC delivery systems.

Controlling Supramolecular Chiral Nanostructures by Self-Assembly of a Biomimetic ß-Sheet-Rich Amyloidogenic Peptide.

Squid sucker ring teeth (SRT) have emerged as a promising protein-only, thermoplastic biopolymer with an increasing number of biomedical and engineering applications demonstrated in recent years. SRT is a supra-molecular network whereby a flexible, amorphous matrix is mechanically reinforced by nanoconfined ß-sheets. The building blocks for the SRT network are a family of suckerin proteins that share a common block copolymer architecture consisting of amorphous domains intervened by smaller, ß-sheet forming modules. Recent studies have identified the peptide A1H1 (peptide sequence AATAVSHTTHHA) as one of the most abundant ß-sheet forming domains within the suckerin protein family. However, we still have little understanding of the assembly mechanisms by which the A1H1 peptide may assemble into its functional load-bearing domains. In this study, we conduct a detailed self-assembly study of A1H1 and show that the peptide undergoes ß-strands-driven elongation into amyloid-like fibrils with a rich polymorphism. The nanostructure of the fibrils was elucidated by small and wide-angle X-ray scattering (SAXS and WAXS) and atomic force microscopy (AFM). The presence of His-rich and Ala-rich segments results in an amphiphilic behavior and drives its assembly into fibrillar supramolecular chiral aggregates with helical ribbon configuration in solution, with the His-rich region exposed to the solvent molecules. Upon increase in concentration, the fibrils undergo gel formation, while preserving the same mesoscopic features. This complex phase behavior suggests that the repeat peptide modules of suckerins may be manipulated beyond their native biological environment to produce a wider variety of self-assembled amyloid-like nanostructures.