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

Qi Gao, Yuqiang Fang, Shiqing ZHANG, Hung Wing LI, Kin Lam YUNG, King Wai Chiu Lai*

*Corresponding author for this work

Research output: Contribution to journalJournal articlepeer-review

2 Citations (Scopus)


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 Aβ 1-40 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. Aβ 1-40 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 Aβ 1-40 oligomer treatment, possibly resulting inmicrotubule disassembly. This paper demonstrates the linkage between cellular mechanical changes and neurodegeneration mediated by Aβ 1-40. The method used implies promising applications of real-time monitoring of cellular mechanical properties given the toxic effects of Aβ 1-40 on living neuronal cells.

Original languageEnglish
Pages (from-to)70-77
Number of pages8
JournalIEEE Transactions on Nanobioscience
Issue number1
Publication statusPublished - Jan 2018

Scopus Subject Areas

  • Biotechnology
  • Bioengineering
  • Medicine (miscellaneous)
  • Biomedical Engineering
  • Pharmaceutical Science
  • Computer Science Applications
  • Electrical and Electronic Engineering

User-Defined Keywords

  • atomic force microscopy
  • Beta amyloid
  • cellular mechanics


Dive into the research topics of 'Biophysical Characteristics of Human Neuroblastoma Cell in Oligomeric β-Amyloid (1-40) Cytotoxicity'. Together they form a unique fingerprint.

Cite this