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

Y Cao, R Mezzenga - Advances in colloid and interface science, 2019 - Elsevier
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 …

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology

G Wei, Z Su, NP Reynolds, P Arosio… - Chemical Society …, 2017 - pubs.rsc.org
Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …

[HTML][HTML] Amyloid-polysaccharide interfacial coacervates as therapeutic materials

M Peydayesh, S Kistler, J Zhou, V Lutz-Bueno… - Nature …, 2023 - nature.com
Coacervation via liquid-liquid phase separation provides an excellent opportunity to address
the challenges of designing nanostructured biomaterials with multiple functionalities. Protein …

Technological functionality and biological properties of food protein nanofibrils formed by heating at acidic condition

M Mohammadian, A Madadlou - Trends in Food Science & Technology, 2018 - Elsevier
Background Nanofibrillation of proteins by heating at extremely acidic condition for long
durations (several hours to days) is studied enthusiastically in food science. The process …

Protein nanofibrils and their use as building blocks of sustainable materials

C Lendel, N Solin - RSC advances, 2021 - pubs.rsc.org
The development towards a sustainable society requires a radical change of many of the
materials we currently use. Besides the replacement of plastics, derived from petrochemical …

Food protein-derived amyloids do not accelerate amyloid β aggregation

MM Rahman, RS Pires, A Herneke, V Gowda… - Scientific Reports, 2023 - nature.com
The deposition of proteins in the form of amyloid fibrils is closely associated with several
serious diseases. The events that trigger the conversion from soluble functional proteins into …

Assembly of iron-bound ovotransferrin amyloid fibrils

Z Wei, Q Huang - Food Hydrocolloids, 2019 - Elsevier
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 …

Evaluation of protease resistance and toxicity of amyloid-like food fibrils from whey, soy, kidney bean, and egg white

M Lassé, D Ulluwishewa, J Healy, D Thompson… - Food Chemistry, 2016 - Elsevier
The structural properties of amyloid fibrils combined with their highly functional surface
chemistry make them an attractive new food ingredient, for example as highly effective …

Rosmarinic acid restrains protein glycation and aggregation in human serum albumin: multi spectroscopic and microscopic insight-possible therapeutics targeting …

A Shamsi, A Ahmed, MS Khan, FM Husain… - International Journal of …, 2020 - Elsevier
Protein aggregation and glycation are directly associated with many pathological conditions
including several neurodegenerative disorders. This study investigates the potential of …

Biophysical elucidation of fibrillation inhibition by sugar osmolytes in α-lactalbumin: multispectroscopic and molecular docking approaches

S Bashir, A Shamsi, F Ahmad, MI Hassan, MA Kamal… - Acs Omega, 2020 - ACS Publications
Protein aggregation is among the most challenging new frontiers in protein chemistry as well
as in molecular medicine and has direct implications in protein misfolding. This study …