We report for the very first time the discovery of amyloid-like self-assemblies formed by the nonaromatic single amino acids cysteine (Cys) and methionine (Met) under neutral aqueous conditions. The structure formation was assessed and characterized by various microscopic and spectroscopic techniques such as optical microscopy, phase contrast microscopy, scanning electron microscopy, and transmission electron microscopy. The mechanism of self-assembly and the role of hydrogen bonding and thiol interactions of Cys and Met were assessed by Fourier transform infrared spectroscopy, thermogravimetric analysis, X-ray diffraction, and solid state NMR along with various control experiments. In addition, molecular dynamics simulations were carried out to gain insight into assembly initiation. Further, Thioflavin T and Congo red binding assays with Cys and Met structures indicated that these single amino acid assemblies may have amyloid-like characteristics. To understand the biological significance of the Cys and Met structures, cytotoxicity assays of the assemblies were performed on human neuroblastoma IMR-32 cells and monkey kidney cells (COS-7). The results revealed that both Cys and Met fibers were cytotoxic. The cell viability assay further supported the hypothesis that aggregation of single amino acid may contribute to the etiology of metabolic disorders like cystinuria and hypermethioninemia. The results presented in this study are striking, and to the best of our knowledge this is the first report which demonstrates that nonaromatic amino acids like Cys and Met can undergo spontaneous self-assembly to form amyloidogenic aggregates. The results presented are also consistent with the established generic amyloid hypothesis and support a new paradigm for the study of the etiology of single amino acid initiated metabolic disorders in amyloid related diseases.

We report for the first time self-assembly of an acyl-thiourea based sensor, N-{(6-methoxy-pyridine-2-yl) carbamothioyl}benzamide (NG1) to panchromatic fluorescent fibres and its dual-sensing properties for the sequential detection of Cu2+ ions...

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A supramolecular cucurbit[6]­uril (CB[6])-enriched magnetic montmorillonite (CBCM) nanocomposite was prepared and characterized. CB[6] played a prominent role as a capping agent, helping in better distribution of the nanoparticles, and as a binder between nanoparticles. Montmorillonite provided structural stability and fortified ultrafast adsorption toward dyes. Its application in the removal of cationic dyes from wastewater was systematically assessed. Process parameters such as pH, initial dye concentration, dosage, temperature, and time were optimized. Kinetics and isotherms of the process were described using pseudo-second-order kinetics and the Langmuir isotherm, respectively. CBCM exhibited rapid dye removal capacity in short reaction times with q max of 199.20, 78.31, and 55.62 mg g–1 and K2 of 0.0281, 0.0.0823, and 0.0953 L mg–1 min–1 for crystal violet, methylene blue, and rhodamine B, respectively. Benefiting from the synergetic effects of montmorillonite surface hydrophobicity, abundant carbonyl groups of CB[6], and magnetic properties of copper ferrite, CBCM demonstrated outstanding dye removal capacity, negligible leaching at saturation, and high tolerance toward harsh conditions. This intrinsic nature is expedient in prolonged industrial operations. To demonstrate industrial viability, syringe filtration and continuous flow fixed-bed column operations were validated. The CBCM fixed-bed column demonstrated stable dye removal efficiency with 10–100 mg mL–1 dye at 10–50 mL min–1 flow rates. Utilizing the magnetic and catalytic activities of the copper ferrite nanoparticles, CBCM was recycled using a magnet, regenerated, and reused for several cycles. CB[6] remarkably improved the performance of the nanocomposite and made it suitable for different effluent treatment techniques. This may pave a sustainable way toward the efficient onsite treatment of effluent at the industrial scale.

Aggregation of amyloid beeta 1-42 (Aβ₄₂) peptide causes the formation of clustered deposits knows as amyloid plaques in the brain which leads to neuronal dysfunction and memory loss and associated with many neurological disorders including Alzheimer’s and Parkinson’s. Aβ₄₂ has core structural motif with phenylalanine at the 19 and 20 positions. The diphenylalanine (FF) residue plays a crucial role in the formation of amyloid fibers and serves as model peptide for studying Aβ₄₂aggregation. FF self-assembles to well-ordered tubular morphology via aromatic pi-pi stackings. Our studies, suggest that the aromatic rings present in the anti-amyloidogenic compounds may interact with the pi-pi stacking interactions present in the FF. Even the compounds which do not have aromatic rings, like cyclodextrin and cucurbituril show anti-amyloid property due to the binding of aromatic ring inside the guest cavity. Hence, our studies also suggest that compounds which may have a functional moiety capable of interacting with the aromatic stacking interactions might be tested for their anti-amyloidogenic properties. Further, in this manuscript, we have proposed two novel nanoparticle based assays for the rapid screening of amyloid inhibitors. In the first assay, interaction between biotin-tagged FF peptide and the streptavidin labelled gold nanoparticles (s-AuNPs) were used. In another assay, thiol-Au interactions were used to develop an assay for detection of amyloid inhibitors. It is envisaged that the proposed analytical method will provide a simple, facile and cost effective technique for the screening of amyloid inhibitors and may be of immense practical implications to find the therapeutic remedies for the diseases associated with the protein aggregation.