Unraveling Amyloid Formation and Heterogeneity by AFM Single Molecule Statistical Analysis скачать в хорошем качестве

Unraveling Amyloid Formation and Heterogeneity by AFM Single Molecule Statistical Analysis

The understanding of the mechanisms of amyloids formation and polymorphism is of fundamental importance to gain biophysical insights into the potential toxicity of the intermediate aggregation species. The comprehension of these fundamental processes could allow the design of pharmacological approaches to contrast the onset of amyloid diseases. Atomic Force Microscopy (AFM) has emerged in the last decades as one of the most powerful and versatile single molecule techniques because of the possibility to acquire 3-dimensional morphology maps of specimens on a surface. This capability has been widely used in the field of protein aggregation and amyloid fibrils formation. Dr. Ruggeri explains in the webinar how a simple AFM map can provide extremely valuable information at the nanometer scale on the structure of amyloid fibrils, such as height, width, periodicity, flexibility and packing of single protofilaments inside mature fibrils. Furthermore, he shows that the possibility to analyze the morphology at several time points, during the process of amyloid aggregation, enables to shed light on the mechanisms of protein misfolding, on the pathway of fibrillization and the hierarchical polymorphic process of assembly. https://www.parksystems.com/medias/na...