Abstract
Alzheimer’s disease (AD) is a significant contributor to cognitive decline and is responsible for about half of the cases of dementia in later life. Although exact etiology of AD is not known, however, many risk factors for AD are identified. Anesthesia for elderly patients is considered as a risk factor in AD as they frequently experience deterioration in cognitive function with long exposure to anesthetics during surgery. Inhaled anesthetic agents remain the mainstay for patients undergoing major surgical operations. This study using multidimensional NMR spectroscopy provides the first direct evidence in vitro that inhaled anesthetic, halothane specifically interacts with Aβ40 and Aβ42 peptide. Halothane induces structural alternation of Aβ peptide from soluble monomeric α-helical form to oligomeric β-sheet conformation, which may hasten the onset of AD. Aβ42 is more prone to oligomerization compared to Aβ40 in the presence of halothane. The molecular mechanism of halothane induced structural alternation of Aβ peptide is discussed.
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Acknowledgments
Pravat K Mandal acknowledges the financial support, in the form of research grants from the American Health Assistance Foundation, American Parkinson Disease Association and Alzheimer Disease Research Center, University of Pittsburgh.
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An erratum to this article can be found at http://dx.doi.org/10.1007/s11064-007-9476-9
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Mandal, P., Pettegrew, J., McKeag, D. et al. Alzheimer’s Disease: Halothane Induces Aβ Peptide to Oligomeric Form—Solution NMR Studies. Neurochem Res 31, 883–890 (2006). https://doi.org/10.1007/s11064-006-9092-0
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DOI: https://doi.org/10.1007/s11064-006-9092-0