Thursday April 5, 10:59 am Eastern Time
Press Release
SOURCE: Prana Biotechnology Limited
Scientific Research Paper Published in the Journal of Biological
Chemistry Supporting Similarities Between A-Beta and Superoxide
Dismutase
Prana's Metal Technology Theory for Alzheimer's Disease Supported by Findings
MELBOURNE, Australia, April 5 /PRNewswire Interactive Release/ -- Prana Biotechnology Limited (Nasdaq: PRNAF;
ASX: PBT) today announced that the research paper titled ``Alzheimer's Disease Amyloid Beta Binds Cu and Zn to Generate
an Allosterically-ordered Membrane-penetrating Structure Containing SOD-like Subunits,'' published in the Journal of
Biological Chemistry on March 27, 2001, bolsters Prana's platform theory of metals and amyloid in the treatment of
Alzheimer's disease.
Drs. Colin L. Masters, M.D., executive director of Prana, Ashley I. Bush, M.D., PhD, chief scientific advisor to Prana, Kevin
J. Barnham PhD, chief of structural biology and medicinal chemistry at Prana, and Cyril Curtain, PhD, were part of the ten
scientist team that conducted the research.
``To treat diseases, it's critical to have the right biological target,'' said Prana Biotechnology's Chairman, Geoffrey Kempler.
``This paper, and others to follow, demonstrate that Prana is indeed on the right path and positioned to play a major role in
bringing a treatment for Alzheimer's disease to the market.''
The research highlights their findings that amyloid (the protein associated with Alzheimer's disease), when it binds copper and
zinc, adopts an elegant structure that strongly resembles antioxidant enzyme, superoxide dismutase-like bridging histidine
residues. Moreover, the paper describes how copper and zinc bind amyloid beta peptide, the most important element of
extracellular plaques and perivascular amyloid deposits; inducing aggregation thus giving rise to reactive oxygen species. These
reactions play a highly dangerous role in the disease state, as high concentrations of iron, copper and zinc have been located in
amyloid in disease brains. The scientists demonstrated that coordination of metal ions to amyloid beta peptide is the same in
both aqueous solution and lipid environments.
This effect was abolished if the histidine residues were methylated at nitrogens of the imidazole ring, indicating the presence of
bridging histidine residues, as found in the active site of superoxide dismutase. The end result suggests that metal binding to
amyloid beta peptide generated an allosterically ordered membrane-penetrating oligomer linked by superoxide dismutase-like
bridging histidine residues.
``This is a landmark paper, because, at long last, our long debated theory that A-beta might have a normal function in health as
an SOD-like antioxidant has received respectable recognition for the plausibility of the protein structures that we predicted must
be involved, commented Dr. Bush. ''The findings in the paper will help us determine what are the beneficial functions of
beta-amyloid. These are functions that other treatment approaches for Alzheimer's disease have so far not considered
important. If you knock this protein out with an antibody, let's say, or a secretase enzyme inhibitor, then you might be losing a
subtle but important antioxidant enzyme.``
As of April 4, 2001, Prana Biotechnology announced it has a Level I American Depository Receipt (ADR) program on
Nasdaq. The Company's ADRs are traded over-the-counter under the symbol ``PRNAF.'' One ADR will represents ten Prana
ordinary shares.
The scientific research paper, as published in the Journal of Biological Chemistry, is available at jbc.org. The story
may be referenced, under the heading ``Protein Structure and Fold,'' within the ``JBC Papers in Press Free!'' icon by selecting
``Old News'' for March 27, 2001.
About Prana Biotechnology Limited
Based in Australia, incorporated in 1997 and listed on the Australian Stock Exchange in March 2000, Prana Biotechnology
(Nasdaq: PRNAF; ASX: PBT) was established to commercialize research into Alzheimer's disease and other major
age-related degenerative disorders. Its mission is to develop therapeutic drugs to treat the central disease pathways that cause
degeneration of the brain and eyes as the aging process progresses. Prana's technology has emerged from its researchers at
prominent international institutions such as Massachusetts General Hospital at Harvard Medical School and the University of
Melbourne. For further information, please visit our web site at pranabio.com.
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SOURCE: Prana Biotechnology Limited |
