2020
DOI: 10.1080/07391102.2020.1798814
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Shear-induced aggregation of amyloid β (1–40) in a parallel plate geometry

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Cited by 17 publications
(12 citation statements)
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“…Further, the conformation changes of the combined heat and UV treated IgG at the above optimized condition (70 °C for 15 minutes) were analyzed as compared to the native IgG using Fourier Transform Infrared Spectroscopy (FTIR) analysis. The FTIR spectra of native and heat treated IgG are shown in Figure 5 , which were de-convoluted and the area of de-convoluted peaks have been used to deduce the contents of the secondary structure ( Sharma et al, 2020 ). The contents of α-helix, β-sheet and β-turn in native IgG were found to be 32, 55 and 13 %, respectively, which agreed with the reported data ( Hasan et al, 2018 ).…”
Section: Resultsmentioning
confidence: 99%
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“…Further, the conformation changes of the combined heat and UV treated IgG at the above optimized condition (70 °C for 15 minutes) were analyzed as compared to the native IgG using Fourier Transform Infrared Spectroscopy (FTIR) analysis. The FTIR spectra of native and heat treated IgG are shown in Figure 5 , which were de-convoluted and the area of de-convoluted peaks have been used to deduce the contents of the secondary structure ( Sharma et al, 2020 ). The contents of α-helix, β-sheet and β-turn in native IgG were found to be 32, 55 and 13 %, respectively, which agreed with the reported data ( Hasan et al, 2018 ).…”
Section: Resultsmentioning
confidence: 99%
“…The software resulted in 13 different combinations of input variables (time and temperature). The hydrodynamic sizes obtained through dynamic light scattering (DLS), optical density at 280 nm (OD 280 ) and intrinsic fluorescence were considered as response variables, which reflect the unfolding of the protein ( Sharma & Pandey, 2021 ; Sharma et al, 2020 ).…”
Section: Methodsmentioning
confidence: 99%
“…Amyloidogenesis in functional, applied, and disease-related situations is dependent on the dynamics of the microenvironment. Fluid interfaces (gas–liquid or liquid–liquid) are an important aspect of the protein environment, which have been shown to significantly influence amyloidogenesis through alterations to energetics/hydrophobicity and protein stability, nucleation and elongation, and surface protein concentration. While the presence and properties of an undisturbed fluid interface affect amyloidogenesis, fluid interfaces in biological systems are often subject to forces, such as fluid shear, which further influence amyloidogenesis kinetics. Fluid shear increases the induction and fibrillization rate of amyloidogenesis in multiple types of amyloid proteins and flow geometries. Previous research in systems with fluid interfaces also indicates that shear normal to the interface drives amyloidogenesis. , Additionally, shear flow is relevant to biological interfaces, such as those in the brain, and the neurological disorders caused by several of the aforementioned amyloid diseases. Specifically, the flow of cerebrospinal fluid, clearance, or accumulation of amyloid fibrils and their precursors, and circulation of amyloid proteins in the brain are fundamental to understanding amyloidogenesis, associated neurodegenerative diseases, and the development of clinical treatments. While the impact of shear flow has been documented in many situations, the effect of interfacially driven shear flow on amyloidogenesis remains unexplored.…”
Section: Introductionmentioning
confidence: 99%
“…Despite the consistently cyclical action of blade reciprocation, the unpredictable variability of fluid velocity entering the cutter port due to viscosity changes and blade dragging results in fragments of extremely variable MW. The increased shear rate created at the cutter port by exceedingly high cut rates may create smaller protein aggregates, 16 thus explaining the reduced proportion of proteins of less than 50 kDa ( Fig. 2 ).…”
Section: Discussionmentioning
confidence: 99%