2018
DOI: 10.1039/c8nj03194k
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Inhibition of amyloid fibril formation of β-lactoglobulin by natural and synthetic curcuminoids

Abstract: The aggregation of proteins has been associated with several aspects of daily life, including food processing, blood coagulation and many neurodegenerative infections.

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Cited by 11 publications
(5 citation statements)
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“…To gain more insight, atomic force microscopy was also employed; it has been proved to be a powerful tool in the study of fibril formation. 27 AFM analysis was performed to visualize the extent of disruption of β-lg samples aggregated alone or with coumarin derivatives at molar concentration ratios of 1 : 1.…”
Section: Resultsmentioning
confidence: 99%
“…To gain more insight, atomic force microscopy was also employed; it has been proved to be a powerful tool in the study of fibril formation. 27 AFM analysis was performed to visualize the extent of disruption of β-lg samples aggregated alone or with coumarin derivatives at molar concentration ratios of 1 : 1.…”
Section: Resultsmentioning
confidence: 99%
“…Docking study is a tool, generally used to predict the position and binding interactions of molecule into proteins or DNAs. 67,68 Among the four methionine amino acids of β-lg, Met7 is located at the surface of the protein and easy to oxidize, Met24 and Met107 are located inside the hydrophobic calyx of β-lg and Met145 is also in the hydrophobic core ( Fig. 6 ).…”
Section: Resultsmentioning
confidence: 99%
“…ThT is a cationic dye having a benzothiazole nucleus that binds strongly with the crossed b-sheet structure of the amyloid fibrils and causes a remarkable enhancement of the emission maxima. 46,47 ThT stock solution of 3.136 mM (1 mg mL À1 ) was prepared by dissolving ThT in HPLC water. From each set of heat incubated and control solutions, aliquots were withdrawn and mixed with ThT solution.…”
Section: Thioflavin T (Tht) Fluorescence Measurementsmentioning
confidence: 99%