Multi-round recycling of green waste for the production of iron nanoparticles: synthesis, characterization, and prospects in remediation.

Due to the widespread applications of metal nanoparticles (NPs), green synthesis strategies have recently advanced, e.g., methods that utilize extracts made from different plant wastes.

Peppermint extract inhibits protein aggregation.

The extracts of 7 herbs were screened and compared for their functional ability to inhibit the aggregation of trypsin as an appropriate model protein for in vitro fibrillation in aqueous ethanol at pH 7.0. Turbidity measurements, total phenolic content determination, aggregation kinetics, Congo red binding assay as well as transmission electron microscopy were used to analyse the inhibition of amyloid fibril formation.

Fruit juices are effective anti-amyloidogenic agents.

Amyloid fibril formation has been associated with a great variety of human diseases. Fruits contain different important bioactive molecules without causing various undesirable side effects, which are necessary for disease prevention and treatment. Here we report that various fruit juices inhibited the amyloid formation by α-chymotrypsin in aqueous ethanol at pH 7.

Coffee extracts effectively inhibit the formation of α-chymotrypsin amyloid-like fibrils in aqueous ethanol in vitro.

In this study, an in vitro α-chymotrypsin aggregation model was used to demonstrate that certain extracts of commercial coffees effectively inhibit protein aggregation in 55% ethanol at pH 7.0. To detect the anti-amyloidogenic effect of the various coffee extracts, turbidity measurements and Congo red binding assays were performed as well as the determination of the total polyphenol content of the extracts.

Inhibition of the formation of amyloid-like fibrils with spices, especially cloves.

During the study of inhibition of amyloid fibril formation, α-chymotrypsin protein was developed in 55% ethanol at pH 7.0. We investigated the inhibitory effect of different spices on amyloid fibril formation using turbidity measurements and Congo red binding assays.

Inhibition of the formation of amyloid-like fibrils using herbal extracts.

We tested the amyloid fibril formation inhibitory effect of seven teas diluted in 55% ethanol at pH 7.0 at a protein concentration of 0.15 mg/ml α-chymotrypsin.

The Inhibitory Effect of Panax Ginseng Extract on Amyloid-like Fibril Formation of Trypsin in Aqueous Ethanol.

Background: In case of several chronic diseases, prevention is could be more effective than treatment. Functional foods that contain significant amounts of bioactive components gained considerable attention not only in traditional but in modern medicine as well. We have investigated how P.

Inhibition of Amyloid-like Fibril Formation of Trypsin by Red Wines.

The aim of the present study was to examine the potential role and applicability of dietary supplements in reducing the risk of development of amyloid diseases associated with the gastrointestinal tract, such as type II diabetes. Trypsin, a well-known serine protease was used as a model protein in our experiments. The effect of various red wines on the formation of amyloid-like fibrils of trypsin was studied in vitro, in aqueous ethanol, at pH 7.

Amyloid-like Fibril Formation by Trypsin in Aqueous Ethanol. Inhibition of Fibrillation by PEG.

The formation of amyloid-like fibrils was studied by using the well-known serine protease trypsin as a model protein in the presence of ethanol as organic solvent. Trypsin forms amyloid-like fibrils in aqueous ethanol at pH = 7.0.

The formation of amyloid-like fibrils of α-chymotrypsin in different aqueous organic solvents.

The formation of amyloid-like fibrils of α-chymotrypsin was studied in aqueous ethanol, methanol, tertbutanol, dimethylformamide and acetonitrile. Thioflavin T (ThT), Congo red (CR) and 1-anilino-8-naphthalenesulfonic acid (ANS) binding, turbidity, intrinsic fluorescence and far-UV circular dichroism measurements were employed to characterize the amyloid fibril formation. The greatest extent of fibril formation after incubation for 24 h at pH 7.

The effects of Al(III) speciation on the activity of trypsin.

The effects of the different forms of Al(III) on the catalytic activity of the serine protease trypsin were studied. Enzyme activity was measured by BAEE assay in the presence of AlCl(3), Al(III):lactic acid 1:3, Al(III):maltol 1:3 or Al(III):nitrilotriacetic acid (NTA) 1:1 at a nominal Al(III) concentration of 0.01 M, and the ligand alone at pH 7.