Fibrillar aggregates in powdered milk.

This research paper addresses the hypothesis that powdered milk may contain amyloid fibrils. Amyloids are fibrillar aggregates of proteins. Up to this time, research on the presence of amyloids in food products are scarce.

Influence of Urea and Dimethyl Sulfoxide on K-Peptide Fibrillation.

Protein fibrillation leads to formation of amyloids-linear aggregates that are hallmarks of many serious diseases, including Alzheimer's and Parkinson's diseases. In this work, we investigate the fibrillation of a short peptide (K-peptide) from the amyloidogenic core of hen egg white lysozyme in the presence of dimethyl sulfoxide or urea. During the studies, a variety of spectroscopic methods were used: fluorescence spectroscopy and the Thioflavin T assay, circular dichroism, Fourier-transform infrared spectroscopy, optical density measurements, dynamic light scattering and intrinsic fluorescence.

DMSO and TMAO-Differences in Interactions in Aqueous Solutions of the K-Peptide.

Interactions between a solvent and their co-solute molecules in solutions of peptides are crucial for their stability and structure. The K-peptide is a synthetic fragment of a larger hen egg white lysozyme protein that is believed to be able to aggregate into amyloid structures. In this study, a complex experimental and theoretical approach is applied to study systems comprising the peptide, water, and two co-solutes: trimethylamide -oxide (TMAO) or dimethyl sulfoxide (DMSO).

Influence of stabilizing osmolytes on hen egg white lysozyme fibrillation.

Communicated by Ramaswamy H. Sarma.

Amyloid fibril formation in the presence of water structure-affecting solutes.

The impact of the differently hydrated non-electrolytes (protein structure destabilizers) on the fibrillation of hen egg white lysozyme (HEWL) was investigated. Two isomeric urea derivatives i.e.

Monitoring of lysozyme thermal denaturation by volumetric measurements and nanoDSF technique in the presence of N-butylurea.

The results of thermal studies of denaturation of hen egg white lysozyme (HEWL) in water and an aqueous solution of N-butylurea (BU) are presented. High-precision densimetric measurements were used to characterize and analyze the changes of the specific volume, v, during temperature elevation. The temperature of the midpoint of protein denaturation was also determined by nanoDSF technique (differential scanning fluorimetry).

How to stop salami science: promotion of healthy trends in publishing behavior.

The career of scientists often depends on the number of their published works. This fact leads to the overproduction of low-quality papers burying the important articles and making the knowledge less accessible. One of the methods to counteract these negative aspects might lie in the promotion of healthy trends in publishing behavior.

Influence of the ionic strength on the amyloid fibrillogenesis of hen egg white lysozyme.

The study investigates the role of the electrostatic interactions in the fibrillation of the hen egg white lysozyme (HEWL). In order to achieve this aim the influence of the cations Na, Mg and Al on the amyloid fibril formation and amorphous aggregation was tested. The amyloids are formed in the solution without added salt but the Thioflavin T fluorescence gives the false-negative result.

Inhibition of amyloid fibril formation of hen egg white lysozyme by trimethylamine N-oxide at low pH.

In vitro inhibition of the formation of fibrous aggregates of proteins (amyloids) has gained increasing attention due to the number of diseases associated with protein misfolding and fibrillation. An interesting group of compounds for which pronounced activity against this phenomenon can be expected consists of low molecular weight substances (osmolytes) which have the ability to change protein stability. Here we investigate the influence of trimethylamine N-oxide (TMAO) in acidic solution (pH=2) on the fibrillation of hen egg white lysozyme (HEWL).