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(Received for publication, February 19, 1997, and in revised form, August 8, 1997)
From the The heterogeneous precipitates of A
Volume 272, Number 42,
Issue of October 17, 1997
pp. 26464-26470
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Zinc-induced Alzheimer's A
1-40 Aggregation Is Mediated by
Conformational Factors
,
,
,
Department of Psychiatry and the Genetics
and Aging Unit, § Department of Pathology, and
¶ Department of Neurology and the Genetics and Aging Unit, Harvard
Medical School, Massachusetts General Hospital,
Boston, Massachusetts 02114
that
accumulate in the brain cortex in Alzheimer's disease possess varying
degrees of resistance to resolubilization. We previously found that
A1-40 is rapidly precipitated in vitro by physiological
concentrations of zinc, a neurochemical that is highly abundant in
brain compartments where A is most likely to precipitate. We now
present evidence that the zinc-induced precipitation of A is
mediated by a peptide dimer and favored by conditions that promote
-helical and diminish -sheet conformations. The manner in which
the synthetic peptide is solubilized was critical to its behavior
in vitro. Zinc-induced A aggregation was dependent upon
the presence of NaCl, was enhanced by -helical-promoting solvents,
but was abolished when the peptide stock solution was stored frozen.
The A aggregates induced by zinc were reversible by chelation, but
could then be reprecipitated by zinc for several cycles, indicating
that the peptide's conformation is probably preserved in the
zinc-mediated assembly. In contrast, A aggregates induced by low pH
(5.5) were not resolubilized by returning the pH milieu to 7.4. The
zinc-A interaction exhibits features resembling the gelation process
of zinc-mediated fibrin assembly, suggesting that, in events such as
clot formation or injury, reversible A assembly could be
physiologically purposive. Such a mechanism is contemplated in the
early evolution of diffuse plaques in Alzheimer's disease and suggests
a possible therapeutic strategy for the resolubilization of some forms
of A deposit in the disease.
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