Investigation of Amyloid Structures at Nanoscale via AFM based Dynamic Nanomechncial Microscopy

Research output: Book/anthology/dissertation/reportPh.D. thesisResearch

  • Shuai Zhang, Denmark
Amyloid structures are one important kind of protein aggregations. They are a group of stable misfolded species, other than native states, which have been found to accumulate as plaques on neuron cells. This behavior is considered to associate with tens of human neurodegenerative diseases. On the other hand, outstanding mechanical properties, good biocompatibility and well-order secondary structures make amyloid nanostructures as a type of attractive functional materials. Hence investigating the scheme of amyloid self-assembly and characterizing amyloid structures are both desired in medical and material research. Among kinds of techniques, Atomic force microscopy (AFM) has the advantages in amyloid study, due to the real-space nano-resolution, the possibilities to characterize in physiological condition, and easy operation without staining requirement. The recent developed AFM based dynamic nanomechnical microscopy (DNM) provides the availability to link topography and corresponding nanomechnical properties. This nanomechnical mapping improves the understanding of amyloid self-assembly mechanisms, and it also assists to design the amyloid structure based nanomaterials. In my PhD thesis, I summarized the main methodologies of DNM. I also utilized DNM to explore the path way of amyloid self-assembly, and the substrate effect to the conformation of amyloid structures. Furthermore, 2D peptide based material has also been characterized by DNM.
Original languageEnglish
Number of pages103
Publication statusPublished - 2014

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