DALLAS, April 2 -- Alzheimer's disease is a progressive and common neurodegenerative disorder with widespread brain destruction and no cure. Fourteen research papers on Alzheimer's disease and related issues will be presented here this week at the national meeting of the American Chemical Society, world's largest scientific society.
DESIGNING BETA-AMYLOID PLAQUE INHIBITORS IN ALZHEIMER'S DISEASE
With the aid of high-powered instruments, researchers at Case Western Reserve
University may have found the first step in the formation of toxic plaque
believed responsible for the destruction of neurons in the brains of Alzheimer's
patients. According to Michael G. Zagorski, Ph.D., this information could be
used to design drugs that might prevent either this initial step or its
continuation into Alzheimer's disease. A sequence of 40 to 42 amino acids, a
so-called beta-peptide, is the major protein component that eventually
aggregates and precipitates as plaque -- an insoluble amyloid deposit -- in the
brains of Alzheimer's patients. The Case Western Reserve team has used nuclear
magnetic resonance (NMR) and a technique called circular dichroism to see what
happens as the beta-peptide, which is originally soluble in water, slowly
changes into the insoluble plaque that is toxic to cells. The first step in
this process, which may be triggered by a changing biochemistry as one ages, has now been determined to be the formation of extended chain-like
structures that fold back on themselves to form the toxic structure.
Paper MEDI 211 will be presented by Michael G. Zagorski from 2:55 to 3:35 p.m., Thurs., April 2, in the Convention Center Ballroom A IV, Level 3.
'MOPPING IT ALL UP': A PLAQUE-ATTACK ON ALZHEIMER'S DISEASE
At Queen's University and Neurochem, Inc. in Kingston, Ontario, Canada,
scientists have found about 100 small organic molecules that bind to the
beta-peptide implicated in Alzheimer's disease and subsequently may prevent it
from aggregating into the insoluble plaque. Although no good animal model
exists for Alzheimer's disease, according to Donald F. Weaver, Ph.D.,
researchers are currently testing their compounds in mice with amyloid-laden
spleens. After molecular modeling simulations and extensive structure-activity
relationship determinations, the Canadian group has found a lead molecule that
looks very promising. It "can mop it all up," says Weaver. He cautions,
however, that any human application is at least two years away.
Paper MEDI 214 will be presented by Donald F. Weaver from 4:55 to 5:30 p.m., Thurs., April 2, in the Convention Center Ballroom A IV, Level 3.
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