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J Biol Chem, Vol. 274, Issue 26, 18801-18807, June 25, 1999

Distribution and Fluidizing Action of Soluble and Aggregated Amyloid -Peptide in Rat Synaptic Plasma Membranes

R. Preston Mason, Robert F. Jacob, Mary F. Walter, Pamela E. Mason, Nicolai A. Avdulov^¶, Svetlana V. Chochina^¶, Urule Igbavboa^¶, and W. Gibson Wood^¶

From the  Membrane Biophysics Laboratory, Departments of Medicine and Biochemistry, MCP Hahnemann University School of Medicine, Allegheny Campus, Pittsburgh, Pennsylvania 15212-4772 and the ^¶ Geriatrics Research, Education and Clinical Center, Veterans Affairs Medical Center and the Department of Pharmacology, University of Minnesota School of Medicine, Minneapolis, Minnesota 55417

The effects of soluble and aggregated amyloid -peptide (A) on cortical synaptic plasma membrane (SPM) structure were examined using small angle x-ray diffraction and fluorescence spectroscopy approaches. Electron density profiles generated from the x-ray diffraction data demonstrated that soluble and aggregated A_1-40 peptides associated with distinct regions of the SPM. The width of the SPM samples, including surface hydration, was 84 Å at 10 °C. Following addition of soluble A_1-40, there was a broad increase in electron density in the SPM hydrocarbon core ±0-15 Å from the membrane center, and a reduction in hydrocarbon core width by 6 Å. By contrast, aggregated A_1-40 contributed electron density to the phospholipid headgroup/hydrated surface of the SPM ±24-37 Å from the membrane center, concomitant with an increase in molecular volume in the hydrocarbon core. The SPM interactions observed for A_1-40 were reproduced in a brain lipid membrane system. In contrast to A_1-40, aggregated A_1-42 intercalated into the lipid bilayer hydrocarbon core ±0-12 Å from the membrane center. Fluorescence experiments showed that both soluble and aggregated A_1-40 significantly increased SPM bulk and protein annular fluidity. Physico-chemical interactions of A with the neuronal membrane may contribute to mechanisms of neurotoxicity, independent of specific receptor binding.

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