Related Experiment Video
Updated: Feb 13, 2026

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
Published on: September 28, 2019
Advanced processes for engineering food protein amyloid fibrils: Molecular mechanisms, processing parameters, and
Mohammad Mahdi Rostamabadi1, Fuat Topuz2, Hadis Rostamabadi3
1Department of Food Science and Technology, College of Agriculture, Isfahan University of Technology, Isfahan 84156-83111, Iran.
Food protein amyloid fibrils (PAFs) offer sustainable nano-materials. Novel processing methods provide precise control over PAF structure and function for diverse applications.
Area of Science:
- Materials Science
- Biochemistry
- Food Science
Background:
- Food protein amyloid fibrils (PAFs) are highly ordered, stable nanostructures with potential in food systems and biomaterials.
- Conventional methods for PAF production are slow, energy-intensive, and offer limited structural control.
Purpose of the Study:
- To systematically review emerging processing technologies for PAF production.
- To investigate the molecular mechanisms, parameters, and structure-function relationships of these novel methods.
Main Methods:
- Review of recent advancements in processing technologies including high-pressure, ultrasonication, cold plasma, electric fields, ohmic/microwave heating, UV, RF, pH modulation, and enzymatic hydrolysis.
- Analysis of molecular mechanisms and structure-function interrelationships.
Main Results:
- Emerging technologies offer precise control over fibrillation kinetics, morphology, and functional performance of PAFs.
- These methods overcome limitations of conventional thermal acid-induced fibrillization.
Conclusions:
- Innovative processing routes enable optimized PAF production for advanced nanostructures.
- PAFs hold transformative potential for food, biomedical, and cross-industry applications.
More Related Videos
10:10Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
Published on: December 1, 2020
09:43Purification and Refolding to Amyloid Fibrils of His6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli
Published on: December 19, 2015
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid Fibrils
Structural Protein Function
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
Structural Protein Function
Mechanical Protein Functions
Chromatin Structure Regulates pre-mRNA Processing
The chromatin structure, especially...