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Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications

Advances in Colloid and Interface Science, 2019
Amyloid fibrils have traditionally been considered only as pathological aggregates in human neurodegenerative diseases, but it is increasingly becoming clear that the propensity to form amyloid fibrils is a generic property for all proteins, including ...
Yiping Cao, Raffaele Mezzenga
exaly   +2 more sources

Formation and physicochemical properties of amyloid fibrils from soy protein

International Journal of Biological Macromolecules, 2020
Amyloid-like fibrils from food proteins possess unique functional properties for food and many other uses. This study reports the effect of hydrolytic heating (pH 2.0, 85 °C, 0-24 h) and incubation times (0-7 days) on the formation and physicochemical ...
Yajuan Wang   +2 more
exaly   +2 more sources

Assembly of iron-bound ovotransferrin amyloid fibrils

Food Hydrocolloids, 2019
The impacts of pH, temperature, ionic strength and stirring speed on the assembly of ovotransferrin (OVT) into amyloid fibrils were analyzed by using thioflavin T fluorescence and atomic force microscopy.
Zihao Wei, Qingrong Huang
exaly   +2 more sources

High internal phase emulsions stabilized with amyloid fibrils and their polysaccharide complexes for encapsulation and protection of β-carotene

Colloids and Surfaces B: Biointerfaces, 2019
In present study, lysozyme amyloid fibrils and their complexes with polysaccharides were investigated for stabilizing high internal phase emulsions (HIPEs).
Yingqun Nian   +2 more
exaly   +2 more sources

Inhibition of Amyloid Fibril Growth and Dissolution of Amyloid Fibrils by Curcumin–Gold Nanoparticles

Chemistry - A European Journal, 2014
AbstractInhibition of amyloid fibrillation and clearance of amyloid fibrils/plaques are essential for the prevention and treatment of various neurodegenerative disorders involving protein aggregation. Herein, we report curcumin‐functionalized gold nanoparticles (Au‐curcumin) of hydrodynamic diameter 10–25 nm, which serve to inhibit amyloid fibrillation
Amit Ranjan Maity   +2 more
exaly   +3 more sources

Amyloid and Amyloid Fibrils

2016
When proteins do not fold correctly, it can lead to very serious diseases. One such group of diseases is the amyloid diseases, of which Alzheimer’s disease (AD), Parkinson’s disease, and type 2 diabetes mellitus (T2DM) are members. The amyloid diseases are characterized by the aggregation of a specific protein into amyloid fibrils. During this process,
K. K. Skeby
openaire   +2 more sources

Formation, structure and functional characteristics of amyloid fibrils formed based on soy protein isolates.

International Journal of Biological Macromolecules, 2023
Food protein-derived amyloid fibrils possess great untapped potential applications in food and other biomaterials. The objective of this report was to investigate the formation mechanism, structure and functional characterization of soy protein amyloid ...
Zhichao Yu   +6 more
semanticscholar   +1 more source

Sustainable Removal of Microplastics and Natural Organic Matter from Water by Coagulation-Flocculation with Protein Amyloid Fibrils.

Environmental Science and Technology, 2021
Water contamination is a global threat due to its damaging effects on the environment and human health. Water pollution by microplastics (MPs), dissolved natural organic matter (NOM), and other turbid particles is ubiquitous in water treatment.
Mohammad Peydayesh   +6 more
semanticscholar   +1 more source

Assembly behavior, structural characterization and rheological properties of legume proteins based amyloid fibrils

, 2021
The assembly behavior of three selected legume proteins was monitored using thioflavin T (ThT) fluorescence intensity, atomic force microscopy (AFM) and dynamic light scattering (DLS) in this test.
Ting Li   +5 more
semanticscholar   +1 more source

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