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(Received for publication, July 7, 1997)
From the The interaction of Alzheimer's A
Volume 272, Number 37,
Issue of September 12, 1997
pp. 22987-22990
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
-(1-40) Peptide to Ganglioside-containing Membrane Vesicles
,
Department of Pathology, Case Western
Reserve University, Cleveland, Ohio 44106 and the
§ Department of Molecular Biology and Biochemistry,
University of California, Irvine, California 92696
peptide and
its fluorescent analogue with membrane vesicles was studied by
spectrofluorometry, Congo Red binding, and electron microscopy. The
peptide binds selectively to the membranes containing gangliosides with
a binding affinity ranging from 10
6 to
107 M depending on the type of ganglioside
sugar moiety. This interaction appears to be ganglioside-specific as
under our experimental conditions (neutral pH, physiologically relevant
ionic strength), no A binding was observed to ganglioside-free
membranes containing zwitterionic or acidic phospholipids. Importantly,
the addition of ganglioside-containing vesicles to the peptide solution
dramatically accelerates the rate of fibril formation as compared with
that of the peptide alone. The present results strongly suggest that
the membrane-bound form of the peptide may act as a specific
"template" (seed) that catalyzes the fibrillogenesis process
in vivo.
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