Modulating amyloids’ formation path with sound energy

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 120; no. 3; p. e2212849120
• Main Authors: Kozell, Anna, Eliaz, Dror, Solomonov, Aleksei, Benyamin, Doron, Shmul, Guy, Brookstein, Ori, Rosenhek-Goldian, Irit, Raviv, Uri, Shimanovich, Ulyana
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 17.01.2023
• Subjects: Agglomeration; Amyloid; Amyloid - chemistry; Amyloid beta-Peptides - chemistry; Amyloidogenesis; Amyloidosis; Assemblies; Biological activity; Biological Sciences; Boundary conditions; Damage; Fractions; Humans; Infrared analysis; Lysozyme; Mechanical properties; Modulus of elasticity; Monomers; Muramidase - chemistry; Nucleation; Parameter modification; Perturbation; Physical Sciences; Protein Folding; Protein structure; Proteins; Self-assembly; Sound; Temperature effects; Ultrasonic imaging; Ultrasound; X-ray scattering; fibrillar protein self-assembly; amyloid; beta-sheet conformation; ultrasound; cavitation

Protein folding is crucial for biological activity. Proteins’ failure to fold correctly underlies various pathological processes, including amyloidosis, the aggregation of insoluble proteins (e.g., lysozymes) in organs. The exact conditions that trigger the structural transition of amyloids into β-s...