Peptide assembly is closely related to many degenerative diseases, such as Alzheimer’s disease (AD), Parkinson's disease are associated with . Understanding of the peptide assembly structure and dynamics is crucial for the development of diagnosis and treatment strategies for these diseases. We investigated the assembly structure, the folding structures and their modulation of the disease related amyloid peptides. The folding structures of the human islet amyloid polypeptide (hIAPP) relating to type 2 diabetes, and TAR DNA-binding protein 43 (TDP-43) relating to frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS) are reported. Based on the above understandings, the short peptides binding to the target proteins with high affinity and selectively are designed to inhibit the aggregation of the amyloid peptides. By using the peptide-modified magnetic nanoparticles, efficient isolation and detection of circulating tumor cells are also achieved. The single molecule study on peptide assembly could shed light on the diagnosis and treatment of many important diseases, including amyloidoses and tumors.
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