The severe impact of in vivo-like microfluidic flow and the influence of gemini surfactants on amyloid aggregation of hen egg white lysozyme

Abstract

The formation of amyloid plaques is being intensively studied, as this process underlies severe human diseases, including Alzheimer's disease, and the exact mechanism of this specific aggregation has not been resolved yet.

Clear distinction between CAC and CMC revealed by high-resolution NMR diffusometry for a series of bis-imidazolium gemini surfactants in aqueous solutions

“… 58 Also, it was proven that above CAC the viscosity of surfactant solution decreases significantly, 53 which could probably inhibit the unfavourable process of protein aggregation called amyloidogenesis, which leads to neurodegenerative disorders. 59 …”

“…58 Also, it was proven that above CAC the viscosity of surfactant solution decreases signicantly, 53 which could probably inhibit the unfavourable process of protein aggregation called amyloidogenesis, which leads to neurodegenerative disorders. 59 Additionally, determination of CAC and CMC values for gemini surfactants is essential for optimization of their usage as delivery systems for nucleic acid in gene therapy. 60,61 They are extremely efficient at condensing DNA and RNA molecules and therefore can be used at low concentrations, what reduces the adverse cytotoxicity effects.…”

PrP (58–93) peptide from unstructured N-terminal domain of human prion protein forms amyloid-like fibrillar structures in the presence of Zn2+ ions

“…Insoluble brillar polypeptide structures appear as a result of a misfolding process in numerous proteins or peptides and accompany the amyloid aggregation process. [1][2][3][4][5][6] The most spectacular structures of this type are linked to the development of fatal neurodegenerative disorders such as Alzheimer's disease, 7,8 Icelandic type amyloidosis 9,10 or Creutzfeldt-Jakob disease. 11,12 The latter belongs to the group of diseases called transmissible spongiform encephalopathies (TSE) in which a misfolding of human prion protein (PrP) is responsible for the formation of brillar aggregates in the brain.…”

Microchip Circulation Drastically Accelerates Amyloid Aggregation of 1–42 β-amyloid Peptide from Felis catus

“…The microfluidic system used in the study was composed of a microfluidic chip and a pressure controller for inducing the desired flow. This system was recently successfully tested by us on the lysozyme aggregation process …”

“…Many scientific groups have built microsystems intended to mimic flow of blood in organism vessels. They used a very wide range of diameters, from 16 μm to as much as 1 mm, and flow rates from 0.1 μL/min to 3300 μL/min, with average velocities from 0.1 to 100 mm/s. ,,− …”