Morgellons? Amyloid II Filaria or Artificial Amyloid Nano Tech?


Amyloid from artificial foods, amyloid from calcified dead worms, or amyloid from synthetic materials.    Any which way,  amyloid forms the core of the matrix that either destroys the human, enhances the artificial program, or becomes totally synthetic and artificial and this  matrix  rules, thereby controlling the body operation electrically, magnetically as well as computer aligned.

Calcified worms from Onchocerciasis, Leshmaniasis, Chagas and Mansonella  ozzardi and perstans are all ignored in the US.  They do not exist here, according to our “flawed Health System”.  However, parasites are not looked at very closely at all.   Due to weather modification by Aerosol operations, which can drop anything onto the human or the planet, depending on the program for the day or the certain environmental area, to be made into a desert, flooded or windswept, the temperature is altered by massive cloud cover, or massive droppings of materials from these planes.

By changing the temperature along with the genetic alteration of insects, which are vectors of these worm diseases, these pathogens increase.   Areas that were not tropical, are now tropical, and carry those tropical diseases.   Areas that were tropical, are now cooler.   So, this increases the midges and the altered new species of mosquitoes, carrying the malaria vaccine are now  attacking humans.  These mosquitoes and midges now carry onchocerca volvulus, mansonella ozzardi, mansonella perstans and other symbiotic bacterias like wohlbachia (ricketts form) and the fly larvae itself.   Global climate change produced by chemtrails, has added to this effect in areas where dormant species did not attack humans, now the do.

Amyloid is calcified material.   Worms dying are calcified and create an extreme itching, that causes panniculitis (yellowish water) comes out of skin, this then replaces the skin with a lizard skin.  Many Morgellons people have suffered this and watch as their skin turns to rough, peeling, and/or bleeding tissue.  Lesions appear, as they break open, or remain under the skin as amyloid type nodules.  These go dormant for a time then the larvae of the fly proceeds to hatch.   So, yes, Morgellons folks have seen the flies, and midges are very small.   Not only is one dealing with fly larvae, one is dealing with wohlbachia and the filarial worms themselves, which are from the c. elegans type worm or the artificial worm micelles.

The artificial amyloids do this as well.   So, it is hard to determine if a true parasite, which is never looked for, or amyloid inside the body is tearing apart the organs.  However, Artificial amyloids are used to create the Matrix inside the human body.   This is more of what Morgellons is like.   It can be very much aligned with the filarial diseases, because they act alike. There are different shapes of fibers;  is the black worm the synthetic male elegans? or the red worm the synthetic female elegans?  Are the smaller ones the amyloid fibers which are the filarial forms?   What a system to use?   It is perfect.

Morgellons is not the filarial diseases, it is the mimic of the filarial diseases.   You have an artificial larvae, an artifical bacterial chromosome, an artificial filarial, but you have to have the amyloid core.  Here is an image of an amyloid fibril: from the article below.

The straight fibril that runs from the centre of the picture to the the bottom-right, is 0.5 microns in length (about quarter of the length of an E. coli cell, or 1/2000 of a millimetre). Each of those dots is a sphere of gold that is 5 nanometres in width.

Dressing up biology like a circuit board…

“An alternative route is to work from the ‘bottom-up’; start with the smallest molecules possible, and gradually build a circuit on a nano-scale, which in our lab generally encompasses molecules up to the size of 100 nm (nanometers), which is about 1/10,000th of a millimetre on a ruler. However, how does one go about making electronic circuits that are so small? One way is to use self-assembly, and if there’s one thing that biologists know about, it’s self-assembly. We know that one strand of DNA binds to its complementary strand of DNA, in the form of DNA base-pairs. We know that certain proteins bind to other proteins, or to certain sequences of DNA. By understanding these processes, we can design circuit boards that quite literally self assemble.

In the picture above, this was an attempt to make a single wire (a nanowire) out of a filament of protein, for just such a nano-circuit board. Of course, these filaments are no good for conducting electricity on their own; they are only the scaffold onto which we plaster a metal, such as gold, which does conduct electricity. So, firstly we’ve got to change the properties of the individual proteins that make up the amyloid filaments, so that gold now likes to bind to them; then we can add gold in the form of gold nanoparticles. In the picture above you can see the gold nanoparticles as small spheres, only 5 nanometres wide, each consisting of a cluster of around 100 gold atoms. We buy the gold in a solution, and as the nanoparticles are so small, they just float around, never settling, and appear red coloured to the eye.

Once the gold nanoparticles coat the the amyloid we need to join-the-dots, so to speak. The metal needs to be touching for electricity to pass, so we simply add more gold, but this time free-atomic gold, which fills in the spaces. We then bake the wires at a very high temperature, to melt all the gold into one long wire, and then test to see if it conducts electricity”


Now, to take this further, one can see why the amyloid diseases were never addressed. These became catalyst for the new Change, or the New Human Evolutionary Technology. It has always been on the back burner for Neumann, Feynman and Frietas.  The new molecular machines.   Please note the messages from the following articles and definitions.


 “Amyloid P component, serum (SAP) is the identical serum form of amyloid P component (AP), a 25kDa pentameric protein first identified as the pentagonal constituent of in vivo pathological deposits called “amyloid“.[1] APCS is its human gene

In amyloidosis

AP makes up 14% of the dry mass of amyloid deposits[3] and is thought to be an important contributor to the pathogenesis of a related group of diseases called the Amyloidoses.[4] These conditions are characterised by the ordered aggregation of normal globular proteins and peptides into insoluble fibres which disrupt tissue architecture and are associated with cell death. AP is thought to decorate and stabilise aggregates by preventing proteolytic cleavage and hence inhibiting fibril removal via the normal protein scavenging mechanisms

SAP is a member of the pentraxins family, characterised by calcium dependent ligand binding and distinctive flattened β-jellyroll structure similar to that of the legume lectins.[8] The name “pentraxin” is derived from the Greek word for five (penta) and berries (ragos) relating to the radial symmetry of five monomers forming a ring approximately 95 Å across and 35 Å deep. Human SAP has 51% sequence homology with C-reactive protein (CRP), a classical acute phase response plasma protein, and is a more distant relative to the “long” pentraxins such as PTX3 (a cytokine modulated molecule) and several neuronal pentraxins. Both SAP and CRP are evolutionary conserved in all vertebrates and also found in distant invertebrates such as the horseshoe crab (Limulus polyphemus).[9]

Cathcart ES, Shirahama T, Cohen AS (1967). “Isolation and identification of a plasma component of amyloid”.



Heme Oxygenase-1 is Associated with the Neurofibrillary Pathology of Alzheimer’s Disease

“The increase in heme oxygenase-l protein in association with the neurofibrillary pathology ofAlzheimer’s disease andother diseasescharacterized by neurofibrillary tangles supports the notion that the generation of free radicals andoxidative stress plays a role in the pathogenesis of neurofibrillary pathology. (Am J Pathol 1994, 145:42-47)”



Alzheimer’s disease: microtubule-associated proteins 2 (MAP 2) are not components of paired helical filaments.


In Alzheimer’s disease, the most characteristic neuropathological changes are the formation of neurofibrillary tangles (NFT) and neuritic plaques (NP) characterized by the presence of bundles of paired helical filaments (PHF) that accumulate in the degenerating neurites and neuronal cell bodies. Although the protein composition of the PHF is ill-defined, a number of microtubule-associated proteins have been implicated in these lesions. Here we report results with an antiserum monospecific for the microtubule-associated protein MAP 2 which does not cross-react with any other microtubular protein. Immunostaining with this antibody of sections from an Alzheimer’s brain show a strong reactivity with NFT but no reactivity at the level of the NP. On the other hand, immunostaining of Alzheimer’s brain sections with another antibody specific for the microtubule-associated protein tau shows strong staining of PHF on both NFT and NP. These findings confirm the presence of the tau proteins in the PHF and strongly suggest that MAP 2 may not be a main structural component of the PHF. Labelling of NFT with the anti-MAP 2 antiserum suggests a non-specific binding of MAP 2 to the PHF during the process of NFT formation.


Aggregation and metal-binding properties of mutant forms of the amyloid A beta peptide of Alzheimer’s disease.


A Theory

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Graphical abstract

The PbSe nanoworms have been synthesised from ultra small PbSe nanocrystals at room temperature without any surfactant or template.




An article describing use of amyloid as synthetic material exemplifies this: figure 5: Examples of functional synthetic amyloid materials.From

Nanomechanics of functional and pathological amyloid materials

Amyloid or amyloid-like fibrils represent a general class of nanomaterials that can be formed from many different peptides and proteins. Although these structures have an important role in neurodegenerative disorders, amyloid materials have also been exploited for functional purposes by organisms ranging from bacteria to mammals. Here we review the functional and pathological roles of amyloid materials and discuss how they can be linked back to their nanoscale origins in the structure and nanomechanics of these materials. We focus on insights both from experiments and simulations, and discuss how comparisons between functional protein filaments and structures that are assembled abnormally can shed light on the fundamental material selection criteria that lead to evolutionary bias in multiscale material design in nature.

Subject terms:
Molecular self-assembly

a, Amyloid formation from a native protein results in universal building blocks that can be assembled and functionalized (for example, with fluorophores or metal particles) into larger and more diverse structures. Different structures can be achieved through changes in pH or other processing conditions. b, AFM image of synthetic amyloid fibrils generated in vitro35. cf, The fibrils can assemble to form conducting nanowires (c,d)86, 88, surface coatings (e)91 and nanostructured protein films (f)93. g, Schematic showing a light-harvesting nanostructure generated from amyloid fibrils95. Light harvesting occurs by means of absorption of a photon by the donor (1), followed by non-emissive transfer to an acceptor through resonance energy transfer (2). The energy is released by the acceptor as a photon (3). h, Hollow nanotubes made from amyloid structures could be used to develop new nanoscale antenna96. i, Optical image of active neuron synapses (labelled with a green fluorescent lipophilic probe) whose growth was stimulated by β-sheet-rich scaffolds98. Figure reproduced with permission from: b, ref. 35, © 2007 AAAS; c, ref. 86, © 2006 ACS; d, ref. 88, © 2003 NAS; e, ref. 91, © 2009 NPG; f, ref. 93, © 2010 NPG; g, ref. 95, © 2009 ACS; h, ref. 96, © 2008 RSC; i, ref. 98, © 2000 NAS.



These are the new amyloid constructions, these are what make the amphiphiles and the bolaamphiles, in Morgellons.   The core is the amyloid itself.  So, attempts at this have been made, the result, possibly, was Alzheimers and Morgellons.   Any of the amyloids, are involved in inorganic materials.   These materials are not part of the normal human flora.


Kathryn A. Augustyn





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