期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 134, 期 14, 页码 6061-6063出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja3004478
关键词
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资金
- NIH [GM76201]
- American Health Assistance Foundation
- Glenn Foundation
A hallmark of Alzheimer's disease is the accumulation of insoluble fibrils in the brain composed of amyloid beta (A beta) proteins with parallel in-register cross-beta-sheet structure. It has been suggested that the aggregation of monomeric A beta proteins into fibrils is promoted by seeds that form within compartments of the brain that have limited solvent due to macromolecular crowding. To characterize these seeds, a crowded macromolecular environment was mimicked by encapsulating A beta 40 monomers into reverse micelles. Fourier-transform infrared spectroscopy revealed that monomeric A beta proteins form extended beta-strands in reverse micelles, while an analogue with a scrambled sequence does not. This is a remarkable finding, because the formation of extended beta-strands by monomeric A beta proteins suggests a plausible mechanism whereby the formation of amyloid fibrils may be nucleated in the human brain.
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