Which is something that big pharma is going to be very unhappy about. The holy grail they have been searching for: an alzheimer's drug that stops the disease may actually end up making pharmaceutical companies no money.

I can't post a link, so here's the entire column:

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New Alzheimer's Drug Could Be Effective, Cheap, and Unprofitable

By Alexis Madrigal July 30, 2008 | 2:51:16 PMCategories: Pharmaceutical Industry


An Alzheimer's drug that targets a new area of the brain's circuitry could be a landmark advance in the treatment of dementia, a new study suggests.

And in a surprising twist, scientists first synthesized the drug over a century ago, meaning it cannot be patented by pharmaceutical companies.

The focus of most drug research has been beta-amyloid, a protein which forms sticky clumps outside brain cells, impeding their functioning. But the new drug, Rember, works by breaking up clumps of a different protein, tau, that accumulate inside dying neurons. Tau clumps were long thought a symptom, not a cause, of Alzheimer's.

"This first modestly sized trial in humans is potentially exciting," said Clive Ballard, head of research at the Alzheimer's Society and who was not involved with the research, told The Telegraph. "It suggests the drug could be over twice as effective as any treatment that is currently available."

The company behind Rember, TauRX, presented its study at a massive research conference on dementia, The International Conference on Alzheimer’s Disease, in Chicago. The results have not been published in a peer-review journal yet. But long-time researchers were still impressed with the drug.

Marcelle Morrison-Bogorad, director of Alzheimer's research at the National Institute on Aging, enthused to the AP that the study showed "the first very positive results" she'd seen for stopping mental decline.

By contrast, Alzheimer's treatments targeting beta-amyloid have repeatedly disappointed researchers and biotech companies. For example, last month Myriad Genetics' highly anticipated Flurizan failed to pass its most recent clinical trial. This week, Elan-Wyeth presented worse-than-expected data on its new drug, bapineuzumab. And most currently available treatments seem to offer marginal improvements, at best.

No wonder Rember has researchers excited. It's an even more remarkable outcome for a compound that has been around since the 1800s.

According to the stellar Mind Hacks blog, Rember appears to be a compound, methylene blue, that was first synthesized back in 1876. And that turns out to have huge financial implications.

That's because, as Vaughan Bell explains, no company could patent what could be one of century's blockbuster drugs.

In other words, anyone can make the drug which means its much harder to make money on it as pricing becomes competitive. In contrast, a patent gives you a time-limited monopoly - albeit one that can earn billions.

A widely available cheap generic drug that treats a major disease is actually a fantastic thing for society, but developing them is not typical behaviour for pharmaceutical companies who tend to shun unpatentable drugs.

So Rember could turn out to be cheap and effective, which is great for everyone, except for big pharma, the industry that would probably be needed to produce massive amounts of the drug.

1: Ann Neurol. 2007 Aug;62(2):145-53.

Tau and alpha-synuclein in susceptibility to, and dementia in, Parkinson's
disease.

Goris A, Williams-Gray CH, Clark GR, Foltynie T, Lewis SJ, Brown J, Ban M,
Spillantini MG, Compston A, Burn DJ, Chinnery PF, Barker RA, Sawcer SJ.

Department of Clinical Neurosciences (Neurology Unit), University of Cambridge,
Cambridge, United Kingdom. an.goris@med.kuleuven.be

OBJECTIVE: Parkinson's disease (PD) is a neurodegenerative condition that
typically presents as a movement disorder but is known to be associated with
variable degrees of cognitive impairment including dementia. We investigated the
genetic basis of susceptibility to and cognitive heterogeneity of this disease.
METHODS: In 659 PD patients, 109 of which were followed up for 3.5 years from
diagnosis, and 2,176 control subjects, we studied candidate genes involved in
protein aggregation and inclusion body formation, the pathological hallmark of
parkinsonism: microtubule-associated protein tau (MAPT), glycogen synthase
kinase-3beta (GSK3B), and alpha-synuclein (SNCA). RESULTS: We observed that
cognitive decline and the development of PD dementia are strongly associated (p =
10(-4)) with the inversion polymorphism containing MAPT. We also found a novel
synergistic interaction between the MAPT inversion polymorphism and the single
nucleotide polymorphism rs356219 from the 3' region of SNCA. In our data,
carrying a risk genotype at either of these loci marginally increases the risk
for development of PD, whereas carrying the combination of risk genotypes at both
loci approximately doubles the risk for development of the disease (p = 3 x
10(-6)). INTERPRETATION: Our data support the hypothesis that tau and
alpha-synuclein are involved in shared or converging pathways in the pathogenesis
of PD, and suggest that the tau inversion influences the development of cognitive
impairment and dementia in patients with idiopathic PD. These findings have
potentially important implications for understanding the interface between tau
and alpha-synuclein pathways in neurodegenerative disorders and for unraveling
the biological basis for cognitive impairment and dementia in PD.


PMID: 17683088 [PubMed - indexed for MEDLINE]

1: Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):11213-8.

Selective inhibition of Alzheimer disease-like tau aggregation by phenothiazines.

Wischik CM, Edwards PC, Lai RY, Roth M, Harrington CR.

Cambridge Brain Bank Laboratory, University Department of Psychiatry, United
Kingdom.

In Alzheimer disease (AD) the microtubule-associated protein tau is redistributed
exponentially into paired helical filaments (PHFs) forming neurofibrillary
tangles, which correlate with pyramidal cell destruction and dementia. Amorphous
neuronal deposits and PHFs in AD are characterized by aggregation through the
repeat domain and C-terminal truncation at Glu-391 by endogenous proteases. We
show that a similar proteolytically stable complex can be generated in vitro
following the self-aggregation of tau protein through a high-affinity binding
site in the repeat domain. Once started, tau capture can be propagated by seeding
the further accumulation of truncated tau in the presence of proteases. We have
identified a nonneuroleptic phenothiazine previously used in man (methylene blue,
MB), which reverses the proteolytic stability of protease-resistant PHFs by
blocking the tau-tau binding interaction through the repeat domain. Although MB
is inhibitory at a higher concentration than may be achieved clinically, the
tau-tau binding assay was used to identify desmethyl derivatives of MB that have
Ki values in the nanomolar range. Neuroleptic phenothiazines are inactive. Tau
aggregation inhibitors do not affect the tau-tubulin interaction, which also
occurs through the repeat domain. Our findings demonstrate that biologically
selective pharmaceutical agents could be developed to facilitate the proteolytic
degradation of tau aggregates and prevent the further propagation of tau capture
in AD.

PMCID: PMC38310

According to this article, there are ways to get around the time issue for a patent.

http://pipeline.corante.com/archives...s_comeback.php