Особливості планування і реалізації проектів ресторанного бізнесу

Ресторанний бізнес є однією із найбільш значущих складових індустрії гостинності. Водночас, ресторанний бізнес, з одного боку, є одним із засобів високоліквідного використання капіталу, а з іншого − середовищем із високим ступенем конкурентності. У всьому світі він є одним із найбільш розповсюджених видів малого бізнесу, тому заклади та підприємства ведуть між собою постійну боротьбу за сегментацію ринку, за пошук нових та за утримання постійних споживачів їхньої продукції та послуг. Всі заклади та підприємства повинні мати високий рівень конкурентоспроможності та мати свою унікальність

Hydrophobicity and Conformational Change as Mechanistic Determinants for Nonspecific Modulators of Amyloid β Self-Assembly

The link between many neurodegenerative disorders, including Alzheimer’s and Parkinson’s diseases, and the aberrant folding and aggregation of proteins has prompted a comprehensive search for small organic molecules that have the potential to inhibit such processes. Although many compounds have been reported to affect the formation of amyloid fibrils and/or other types of protein aggregates, the mechanisms by which they act are not well understood. A large number of compounds appear to act in a nonspecific way affecting several different amyloidogenic proteins. We describe here a detailed study of the mechanism of action of one representative compound, lacmoid, in the context of the inhibition of the aggregation of the amyloid β-peptide (Aβ) associated with Alzheimer’s disease. We show that lacmoid binds Aβ(1–40) in a surfactant-like manner and counteracts the formation of all types of Aβ(1–40) and Aβ(1–42) aggregates. On the basis of these and previous findings, we are able to rationalize the molecular mechanisms of action of nonspecific modulators of protein self-assembly in terms of hydrophobic attraction and the conformational preferences of the polypeptide

Selenium-Enhanced Electron Microscopic Imaging of Different Aggregate Forms of a Segment of the Amyloid β Peptide in Cells

The aggregation of misfolded proteins is a common feature underlying a wide range of age-related degenerative disorders, including Alzheimer’s and Parkinson’s diseases. A key aspect of understanding the molecular origins of these conditions is to define the manner in which specific types of protein aggregates influence disease pathogenesis through their interactions with cells. We demonstrate how selenium-enhanced electron microscopy (SE-EM), combined with tomographic reconstruction methods, can be used to image, here at a resolution of 5–10 nm, the interaction with human macrophage cells of amyloid aggregates formed from Aβ_25–36, a fragment of the Aβ peptide whose self-assembly is associated with Alzheimer’s disease. We find that prefibrillar aggregates and mature fibrils are distributed into distinct subcellular compartments and undergo varying degrees of morphological change over time, observations that shed new light on the origins of their differential toxicity and the mechanisms of their clearance. In addition, the results show that SE-EM provides a powerful and potentially widely applicable means to define the nature and location of protein assemblies <i>in situ</i> and to provide detailed and specific information about their partitioning and processing

Additional file 1 of Minimum information and guidelines for reporting a multiplexed assay of variant effect

Additional file 1. Review history