"02nd Feb 2011
Novel approach for isolating disease-causing prions in vitro
Thomas Hauch '13
Researchers at Dartmouth College have made a breakthrough in the fight against prion diseases. Using superparamagnetic nanoparticles, Michael Miller and Surachai Supattapone of the Department of Biochemistry and Medicine have been able to separate infectious prions from a sample mixture. Their findings suggest new possibilities in the detection of prions, as well as the diagnosis and treatment of prion-related diseases.
The word prion is a portmanteau of protein and infection. A prion is, in short, an infectious agent in the form of a misfolded protein. First hypothesized in the 1960s, a prion sample was actually purified and studied until 1982 . Prions are uniquely responsible for transmissible spongiform encephalopathies, a group of degenerative conditions that affect the brain and nervous system in many animals, including humans. These conditions include Bovine spongiform encephalopathy, commonly know as mad cow disease, and Creutzfeldt-Jakob disease, a human neurological disorder that is currently incurable and almost always fatal.
Prions are composed of prion protein, or PrP, a protein which is abundant in healthy tissues. The normal form of this protein is known as PrPc, and it plays an important role in cellular membranes. A prion, or PrPsc, is an infectious isoform of this molecule, capable of altering the shape of normal PrPc proteins. As these denatured proteins accumulate in cells, they begin to aggregate into plaques, causing cell death.
The researchers at Dartmouth were able to isolate these dangerous proteins using superparamagnetic nanoparticles of iron oxide crystals less than ~25nm in diameter. At first glance, these crystals don’t seem to be magnetic. In reality, their magnetization is constantly changing directions quickly enough to go undetected. However, under the influence of an external magnetic field, these nanoparticles are transformed into very powerful agents that are capable of binding to prions.
The researchers performed several studies that examined the efficacy of these nanoparticles in detecting, capturing, and separating prions from sample mixtures. It is well known that distinct strains of prions affect different regions of the nervous system. They possess the same basic amino acid sequence, but display a variety of biochemical properties. The iron oxide nanoparticles were capable of binding to each of the prion samples that were tested. This suggests that the nanoparticles target some general, underlying feature common amongst all PrPsc.
Even more remarkably, these nanoparticles do not bind to the normal PrPc protein. These tests were performed in vitro, as well as in uninfected brain tissue in mice. The findings suggest that nanoparticles are able to capture prions selectively and efficiently. Moreover, they are able to do so without affecting the surrounding environment. Besides nanoparticles, there are other methods of decontaminating biological products of PrPsc. Virtually all of these techniques, however, rely on detergents or acids that are also damaging to the surrounding material, making them useless in applications like sterilizing blood.
Paramagnetic nanoparticles, on the other hand, are small enough that they can safely pass through capillary beds. In fact, they have already been approved for use in magnetic resonance imaging. Unlike other available technique, nanoparticles offer a unique way of simultaneously detecting and decontaminating prion-infected materials and tissues."
Now understand this view-point: if superparamagnetic nanoparticles of a size less than 25 nanometers are capable of "binding" with prion proteins that are NOT already bound with copper ie: PrPc (healthy version), then WHAT HAPPENS when these kinds of paramagnetic nanoparticles find their way into the brain and co-join with the denatured PrPres lying around in the brain (in the process of degradation)?
Sounds very familiar to the work of Mark Purdey, and Dr. Vitaly Vodyanoy.
Another new study of interest:
http://www.mdpi.com/1660-4601/8/6/2200/pdf Free on-line.
Nanoparticles and Colloids as Contributing Factors in Neurodegenerative Disease by Stephen C. Bondy
"Abstract: This review explores the processes underlying the deleterious effects of the presence of insoluble or colloidal depositions within the central nervous system. These materials are chemically unreactive and can have a prolonged residence in the brain. They can be composed of mineral or proteinaceous materials of intrinsic or exogenous origin. Such nanoparticulates and colloids are associated with a range of slow-progressing neurodegenerative states. The potential common basis of toxicity of these materials is discussed. A shared feature of these disorders involves the appearance of deleterious inflammatory changes in the CNS. This may be due to extended and ineffective immune responses. Another aspect is the presence of excess levels of reactive oxygen species within the brain. In addition with their induction by inflammatory events, these may be further heightened by the presence of redox active transition metals to the large surface area afforded by nanoparticles and amphipathic micelles." FREE on-line.
What happens now, when the radio-active contamination/nanoparticles from Fukushima find their way into the livestock of Japan...and the people?
I've heard that livestock in the evacuation zone has been ordered destroyed. Waygu - Wa.. who?
Novel approach for isolating disease-causing prions in vitro
Thomas Hauch '13
Researchers at Dartmouth College have made a breakthrough in the fight against prion diseases. Using superparamagnetic nanoparticles, Michael Miller and Surachai Supattapone of the Department of Biochemistry and Medicine have been able to separate infectious prions from a sample mixture. Their findings suggest new possibilities in the detection of prions, as well as the diagnosis and treatment of prion-related diseases.
The word prion is a portmanteau of protein and infection. A prion is, in short, an infectious agent in the form of a misfolded protein. First hypothesized in the 1960s, a prion sample was actually purified and studied until 1982 . Prions are uniquely responsible for transmissible spongiform encephalopathies, a group of degenerative conditions that affect the brain and nervous system in many animals, including humans. These conditions include Bovine spongiform encephalopathy, commonly know as mad cow disease, and Creutzfeldt-Jakob disease, a human neurological disorder that is currently incurable and almost always fatal.
Prions are composed of prion protein, or PrP, a protein which is abundant in healthy tissues. The normal form of this protein is known as PrPc, and it plays an important role in cellular membranes. A prion, or PrPsc, is an infectious isoform of this molecule, capable of altering the shape of normal PrPc proteins. As these denatured proteins accumulate in cells, they begin to aggregate into plaques, causing cell death.
The researchers at Dartmouth were able to isolate these dangerous proteins using superparamagnetic nanoparticles of iron oxide crystals less than ~25nm in diameter. At first glance, these crystals don’t seem to be magnetic. In reality, their magnetization is constantly changing directions quickly enough to go undetected. However, under the influence of an external magnetic field, these nanoparticles are transformed into very powerful agents that are capable of binding to prions.
The researchers performed several studies that examined the efficacy of these nanoparticles in detecting, capturing, and separating prions from sample mixtures. It is well known that distinct strains of prions affect different regions of the nervous system. They possess the same basic amino acid sequence, but display a variety of biochemical properties. The iron oxide nanoparticles were capable of binding to each of the prion samples that were tested. This suggests that the nanoparticles target some general, underlying feature common amongst all PrPsc.
Even more remarkably, these nanoparticles do not bind to the normal PrPc protein. These tests were performed in vitro, as well as in uninfected brain tissue in mice. The findings suggest that nanoparticles are able to capture prions selectively and efficiently. Moreover, they are able to do so without affecting the surrounding environment. Besides nanoparticles, there are other methods of decontaminating biological products of PrPsc. Virtually all of these techniques, however, rely on detergents or acids that are also damaging to the surrounding material, making them useless in applications like sterilizing blood.
Paramagnetic nanoparticles, on the other hand, are small enough that they can safely pass through capillary beds. In fact, they have already been approved for use in magnetic resonance imaging. Unlike other available technique, nanoparticles offer a unique way of simultaneously detecting and decontaminating prion-infected materials and tissues."
Now understand this view-point: if superparamagnetic nanoparticles of a size less than 25 nanometers are capable of "binding" with prion proteins that are NOT already bound with copper ie: PrPc (healthy version), then WHAT HAPPENS when these kinds of paramagnetic nanoparticles find their way into the brain and co-join with the denatured PrPres lying around in the brain (in the process of degradation)?
Sounds very familiar to the work of Mark Purdey, and Dr. Vitaly Vodyanoy.
Another new study of interest:
http://www.mdpi.com/1660-4601/8/6/2200/pdf Free on-line.
Nanoparticles and Colloids as Contributing Factors in Neurodegenerative Disease by Stephen C. Bondy
"Abstract: This review explores the processes underlying the deleterious effects of the presence of insoluble or colloidal depositions within the central nervous system. These materials are chemically unreactive and can have a prolonged residence in the brain. They can be composed of mineral or proteinaceous materials of intrinsic or exogenous origin. Such nanoparticulates and colloids are associated with a range of slow-progressing neurodegenerative states. The potential common basis of toxicity of these materials is discussed. A shared feature of these disorders involves the appearance of deleterious inflammatory changes in the CNS. This may be due to extended and ineffective immune responses. Another aspect is the presence of excess levels of reactive oxygen species within the brain. In addition with their induction by inflammatory events, these may be further heightened by the presence of redox active transition metals to the large surface area afforded by nanoparticles and amphipathic micelles." FREE on-line.
What happens now, when the radio-active contamination/nanoparticles from Fukushima find their way into the livestock of Japan...and the people?
I've heard that livestock in the evacuation zone has been ordered destroyed. Waygu - Wa.. who?
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