Kathy
Well-known member
My good news is in relation to the science around BSE - go figure!!
First, found this study on how the use of "sonciation" allowed for a better analysis of lead in the brain.
see:
"Epub 2011 Sep 17.
Ultrasonic energy as a tool to overcome some drawbacks in the determination of lead in brain tissue and urine of rats.
Guimarães D, Santos JP, Carvalho ML, Vale G, Santos HM, Geraldes V, Rocha I, Capelo JL."
(From abstract - "Utrasonication provided by an ultrasonic probe succeeded in extracting lead from brain samples.") it extracted more than when not doing this process, thus unveiling the lead trapped inside proteins.
Link to pubmed/abstract:
http://www.ncbi.nlm.nih.gov/pubmed?term=lead%20brain%20urine%20sonication
THIS elucidates a hypothesis that when BSE contaminated brain tissue is homogenated and sonicated before injection, in transmission studies - the process of sonication is likely releasing the metals bound to the proteins and breaking apart the fibrils so their energy (from the metals) is capable of reseeding more fibrils....
EVEN MORE IMPORTANT THOUGH:
Dr. Vitaly Vodyanoy of Auburn University has been granted another patent. The patent gives hope in further research. The patent is:
METHODS FOR ISOLATING PROTEONS FROM PLASMA SAMPLES
USA Patent #8,298,793 granted October 30, 2012.
"Abstract
Compositions and methods for the isolation and manipulation of misfolded, or partially misfolded, proteins present in blood and other biological materials are provided. In one aspect of the invention, the compositions, hereinafter termed "proteons" are misfolded or partially misfolded proteins surrounding a metallic nanocluster, termed "proteon nucleation center" (PNC). Also provided are compositions and methods for the isolation and manipulation of proteon nucleation centers (PNCs) upon which the proteons of the present in blood and other biological materials form."
Go to http://patft.uspto.gov/netahtml/PTO/search-bool.html
and search the patent number, and or Dr. Vitaly Vodyanoy's name to bring up the patent.
This document is a long read but if you go to the end pages you will find information on where all this is leading. For example:
"Hypothesis
Metal clusters (Gonzalez-Morega, 1993; Aiken & Finke, 1999) play a role in the seeds in proteons, Metals involved in the natural folding and misfolding of proteins are not in the ion state, but rather in the clusters of metal atoms. These atoms are directly bonded to each other creating a polyatomic metallic nucleus that can exist alone or are associated with a given number of ligands.
Rationale:
The most remarkable property of metal clusters is that they provide a binding template for folding and aggregation of proteins (Liu and Xu, 2002). High symmetry is one of the main characteristics of metal clusters (Gonzalez-Moraga, 1993). Packing of secondary structures prefers geometrical patterns (Gracy et al., 1993; Onuchic et al., 1997). Many disorders arise from misfolding and aggregation of an underlying protein (Carrel and Lormas, 1997; Sato, 2001). The same disorders were shown to depend on metal misbalance (Bush, 2000). Copper, iron or manganese are involved in the aging and neurological disorders. Metals are involved in prion diseases (Lehman, 2002, Thackray, et al., 2002). Among 327 possible protein folds (Chothia, et al., 1997) only 230 folds are unique. The number of unique space groups applied to inorganic clusters is also equal to 230! (Hahn, 1987). The mathematical accuracy and stability of geometrical patterns and a large number of structural arrangements of metal clusters make them uniquely qualified as perfect templates for protein folding.".....
"What Prions are Proteons?
Proteons and prions share many physical and chemical properties. They both are misfolded proteins, polymorphic, have no nucleic acids, metal dependent, and very resistant. They both may be induced by seeds and be controlled by guanidine hydrochloride. They both play a certain role in a cell death. They both have the same proliferation rate at 37.degree. C. (Aguzzi and Heppner, 2002; Everbroeck, et al., 2002; Ness, et al., 2002; Bounias and PURDEY, 2002; Gemer 1997, 2002). Our experiments with the recombinant human protein described in the section "Proteons from prion protein (PrP)" suggest that metal nanoclusters (PNCs) play important role in production of prion particles. We need to present experimental evidence that metal particles are indeed inside the prions particles. In order to make a statement that naturally occurring prions are proteons, that is to say, natural prion particle is the misfolded prion protein aggregated around non-organic nanoparticle that serves as a nucleating center, it would require to analyze prions obtained from the animal with the prion disease. There is substantial evidence that PrP is a Cu-binding protein. It is suggested that in conversion to the abnormal form the Cu-binding activity is switched to the binding other metals such as Mn or Zn (Brown, 2004). In this work we do not plan to work with prions obtained from animals with prion diseases. We will work with in vitro system of prion particles produced from the recombinant human PrP(23-230) protein and metal PNC and examine if these particles have acquired the ability to convert the normal form of the protein into this same abnormal (prion) form."
There is always an ultimate goal when doing research, and it usually means finding a way to make money from what your doing. Obviously, an accurate test is being sought. But in the search for the test, comes the truth of the disease. Sadly, Dr. Vodyanoy will NOT be working with the actual diseased TSE brain tissue/samples. Why not, I ask?
Please pass on this information to anyone that you know who will shine the light on these developments, especially those at universities, institutes, and even government employees who are doing their own investigations. The more people that know about this, the better. HAPPY NEW YEAR.
First, found this study on how the use of "sonciation" allowed for a better analysis of lead in the brain.
see:
"Epub 2011 Sep 17.
Ultrasonic energy as a tool to overcome some drawbacks in the determination of lead in brain tissue and urine of rats.
Guimarães D, Santos JP, Carvalho ML, Vale G, Santos HM, Geraldes V, Rocha I, Capelo JL."
(From abstract - "Utrasonication provided by an ultrasonic probe succeeded in extracting lead from brain samples.") it extracted more than when not doing this process, thus unveiling the lead trapped inside proteins.
Link to pubmed/abstract:
http://www.ncbi.nlm.nih.gov/pubmed?term=lead%20brain%20urine%20sonication
THIS elucidates a hypothesis that when BSE contaminated brain tissue is homogenated and sonicated before injection, in transmission studies - the process of sonication is likely releasing the metals bound to the proteins and breaking apart the fibrils so their energy (from the metals) is capable of reseeding more fibrils....
EVEN MORE IMPORTANT THOUGH:
Dr. Vitaly Vodyanoy of Auburn University has been granted another patent. The patent gives hope in further research. The patent is:
METHODS FOR ISOLATING PROTEONS FROM PLASMA SAMPLES
USA Patent #8,298,793 granted October 30, 2012.
"Abstract
Compositions and methods for the isolation and manipulation of misfolded, or partially misfolded, proteins present in blood and other biological materials are provided. In one aspect of the invention, the compositions, hereinafter termed "proteons" are misfolded or partially misfolded proteins surrounding a metallic nanocluster, termed "proteon nucleation center" (PNC). Also provided are compositions and methods for the isolation and manipulation of proteon nucleation centers (PNCs) upon which the proteons of the present in blood and other biological materials form."
Go to http://patft.uspto.gov/netahtml/PTO/search-bool.html
and search the patent number, and or Dr. Vitaly Vodyanoy's name to bring up the patent.
This document is a long read but if you go to the end pages you will find information on where all this is leading. For example:
"Hypothesis
Metal clusters (Gonzalez-Morega, 1993; Aiken & Finke, 1999) play a role in the seeds in proteons, Metals involved in the natural folding and misfolding of proteins are not in the ion state, but rather in the clusters of metal atoms. These atoms are directly bonded to each other creating a polyatomic metallic nucleus that can exist alone or are associated with a given number of ligands.
Rationale:
The most remarkable property of metal clusters is that they provide a binding template for folding and aggregation of proteins (Liu and Xu, 2002). High symmetry is one of the main characteristics of metal clusters (Gonzalez-Moraga, 1993). Packing of secondary structures prefers geometrical patterns (Gracy et al., 1993; Onuchic et al., 1997). Many disorders arise from misfolding and aggregation of an underlying protein (Carrel and Lormas, 1997; Sato, 2001). The same disorders were shown to depend on metal misbalance (Bush, 2000). Copper, iron or manganese are involved in the aging and neurological disorders. Metals are involved in prion diseases (Lehman, 2002, Thackray, et al., 2002). Among 327 possible protein folds (Chothia, et al., 1997) only 230 folds are unique. The number of unique space groups applied to inorganic clusters is also equal to 230! (Hahn, 1987). The mathematical accuracy and stability of geometrical patterns and a large number of structural arrangements of metal clusters make them uniquely qualified as perfect templates for protein folding.".....
"What Prions are Proteons?
Proteons and prions share many physical and chemical properties. They both are misfolded proteins, polymorphic, have no nucleic acids, metal dependent, and very resistant. They both may be induced by seeds and be controlled by guanidine hydrochloride. They both play a certain role in a cell death. They both have the same proliferation rate at 37.degree. C. (Aguzzi and Heppner, 2002; Everbroeck, et al., 2002; Ness, et al., 2002; Bounias and PURDEY, 2002; Gemer 1997, 2002). Our experiments with the recombinant human protein described in the section "Proteons from prion protein (PrP)" suggest that metal nanoclusters (PNCs) play important role in production of prion particles. We need to present experimental evidence that metal particles are indeed inside the prions particles. In order to make a statement that naturally occurring prions are proteons, that is to say, natural prion particle is the misfolded prion protein aggregated around non-organic nanoparticle that serves as a nucleating center, it would require to analyze prions obtained from the animal with the prion disease. There is substantial evidence that PrP is a Cu-binding protein. It is suggested that in conversion to the abnormal form the Cu-binding activity is switched to the binding other metals such as Mn or Zn (Brown, 2004). In this work we do not plan to work with prions obtained from animals with prion diseases. We will work with in vitro system of prion particles produced from the recombinant human PrP(23-230) protein and metal PNC and examine if these particles have acquired the ability to convert the normal form of the protein into this same abnormal (prion) form."
There is always an ultimate goal when doing research, and it usually means finding a way to make money from what your doing. Obviously, an accurate test is being sought. But in the search for the test, comes the truth of the disease. Sadly, Dr. Vodyanoy will NOT be working with the actual diseased TSE brain tissue/samples. Why not, I ask?
Please pass on this information to anyone that you know who will shine the light on these developments, especially those at universities, institutes, and even government employees who are doing their own investigations. The more people that know about this, the better. HAPPY NEW YEAR.
