Biophysical Characteristics of Human Neuroblastoma Cell in Oligomeric β-Amyloid (1-40) Cytotoxicity

Research output: Journal Publications and ReviewsRGC 21 - Publication in refereed journalpeer-review

2 Scopus Citations
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  • Yuqiang Fang
  • Shiqing Zhang
  • Hung-Wing Li
  • Ken K. L. Yung


Original languageEnglish
Pages (from-to)70-77
Journal / PublicationIEEE Transactions on Nanobioscience
Issue number1
Publication statusPublished - Jan 2018


Beta amyloid (Aβ) peptide, which is a common neuropathological hallmark deposit in the brain of patients with Alzheimer's disease, typically comprises 39-43 amino acid residues. Aβ peptides exist as isoforms of Aβ1-40 and Aβ1-42 with various lengths. In this research, atomic force microscopy (AFM) was applied to investigate Aβ1-40 aggregations in Hank's Balanced Salt Solution. Toxic effect of Aβ1-40 oligomer was investigated in live SH-SY5Y neuroblastoma cells by characterizing cell morphology and cell mechanics using high-resolution AFM scanning. Aβ1-40 oligomer-induced cytoskeleton reorganization was also observed under confocal microscopy, and it can account for reduction in Young's modulus of cells. Meanwhile, phosphorylation of tau increased after Aβ1-40 oligomer treatment, possibly resulting inmicrotubule disassembly. This paper demonstrates the linkage between cellular mechanical changes and neurodegeneration mediated by Aβ1-40. The method used implies promising applications of real-time monitoring of cellular mechanical properties given the toxic effects of Aβ1-40 on living neuronal cells.

Research Area(s)

  • atomic force microscopy, Beta amyloid, cellular mechanics