AFM-based force spectroscopy measurements of mature amyloid fibrils of the peptide glucagon

摘要: We report on the mechanical characterization of individual mature amyloid fibrils by atomic force microscopy (AFM) and AFM-based single-molecule spectroscopy (SMFS). These self-assembling materials, formed from 29-residue amphiphatic peptide hormone glucagon, were found to display a reversible elastic behaviour. Based AFM morphology SMFS studies, we suggest that observed elasticity is due force-induced conformational transition which β-helical conformation protofibrils, allowing high degree extension. The properties such contribute their stability, suggesting internal hydrophobic interactions are likely be fundamental importance in assembly therefore for understanding progression associated pathogenic disorders. In addition, biological fibril structures with highly stable can potentially used produce nanofibres (nanowires) may suitable nanotechnological applications.