Amyloid fibrils compared to peptide nanotubes

• Published in: Biochimica et biophysica acta Vol. 1840; no. 9; pp. 2944 - 2952
• Main Authors: Zganec, Matjaž, Zerovnik, Eva
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.09.2014
• Subjects: amyloid; Amyloid - chemistry; Amyloid - metabolism; Amyloid - ultrastructure; Amyloid fibrils; cytotoxicity; Humans; nanoparticles; nanotubes; Nanotubes - chemistry; Nanotubes - ultrastructure; neurons; oligomers; optical properties; Peptide nanotubes; Quantum confinement; Toxicity; Quantum confinement; Amyloid fibrils; Peptide nanotubes; optical properties; Toxicity; oligomers
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/j.bbagen.2014.05.019

Prefibrillar oligomeric states and amyloid fibrils of amyloid-forming proteins qualify as nanoparticles. We aim to predict what biophysical and biochemical properties they could share in common with better researched peptide nanotubes. We first describe what is known of amyloid fibrils and prefibrillar aggregates (oligomers and protofibrils): their structure, mechanisms of formation and putative mechanism of cytotoxicity. In distinction from other neuronal fibrillar constituents, amyloid fibrils are believed to cause pathology, however, some can also be functional. Second, we give a review of known biophysical properties of peptide nanotubes. Finally, we compare properties of these two macromolecular states side by side and discuss which measurements that have already been done with peptide nanotubes could be done with amyloid fibrils as well. •Biophysical properties of peptide nanotubes•Piezoelectricity•Second harmonic generation•Biophysical properties of amyloid fibrils