Lysozyme amyloid fibril: Regulation, application, hazard analysis, and future perspectives

Area of Science:

• Biochemistry
• Materials Science
• Neuroscience

Background:

• Amyloid fibrils are ordered aggregates of misfolded proteins linked to human diseases.
• Lysozyme is a model protein extensively studied for amyloid fibril formation.
• Research increasingly identifies amyloidogenic proteins in both biological systems and food.

Purpose of the Study:

• To review the formation mechanisms of lysozyme amyloid fibrils.
• To summarize exogenous substances that regulate lysozyme amyloid fibril formation.
• To explore applications and potential health impacts of lysozyme amyloid fibrils.

Main Methods:

• Review of existing literature on amyloid formation and regulation.
• Analysis of interactions between lysozyme and various exogenous substances (small molecules, nanoparticles, macromolecules, polymers).
• Discussion of the physical and mechanical properties of lysozyme amyloid fibrils.

Main Results:

• Exogenous substances, including small molecules and nanoparticles, can inhibit or modify lysozyme amyloid fibril formation through various interactions (hydrophobic, electrostatic, π-π, van der Waals, hydrogen bonds).
• Nanoparticles stabilize lysozyme and fix β-sheet structures, inhibiting fibril assembly.
• Lysozyme amyloid fibrils exhibit notable physical and mechanical properties, suggesting food-related applications.

Conclusions:

• Understanding lysozyme amyloid fibril formation and regulation is crucial for developing therapeutic strategies and identifying undesirable substances.
• Lysozyme amyloid fibrils have potential applications in the food industry, but their health implications require careful consideration.
• Future research should focus on further elucidating formation mechanisms, regulatory interactions, and safety assessments.