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Logo of jbcThe Journal of Biological Chemistry
J Biol Chem. 2013 June 28; 288(26): 18684.
PMCID: PMC3696642

Teasing out the Structural Details of an Oligomer Involved in Alzheimer Disease♦

Structural Insights into Aβ42 Oligomers Using Site-directed Spin Labeling

♦ See referenced article, J. Biol. Chem. 2013, 288, 18673–18683

A pathological hallmark of Alzheimer disease is the plaques formed by a peptide called Aβ42. Much research has been done on the peptide, including the development of drugs that target it, but the oligomer structures of Aβ42 have not been well characterized. In this Paper of the Week, Zhefeng Guo at the University of California, Los Angeles, and colleagues used site-directed spin labeling combined with other biophysical techniques to characterize the structure of an Aβ42 oligomer called the globulomer. They established that the globulomer was 7–8 nm in diameter and consisted mostly of β-structures with highly ordered intrasheet hydrogen bonding. The investigators concluded that the globulomer consists largely of tightly packed antiparallel β-sheets in the C-terminal region. The authors say, “This work provides insights into the structures of Aβ42 oligomers and helps understand their oligomerization mechanism and toxicity.”

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Transmission electron micrograph of the Aβ42 globulomer.

Articles from The Journal of Biological Chemistry are provided here courtesy of American Society for Biochemistry and Molecular Biology