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Darkfield Microscopy Shows Self Assembly Of Microfilament In C19 Unvaccinated Blood. Are We Seeing Amyloid Fibril Growth Accelerated By Nano/Micro Robots For Biosensing & Electronic Device Creation?

Ana Maria Mihalcea, MD, PhD

Jan 2

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Microfilament undergoing vesicular self assembly in COVID19 unvaccinated blood. Magnification 100x © Dr Ana Mihalcea

In this post, I show multiple videos of Darkfield Microscopy of a filament self assembly in COVID19 unvaccinated blood. This quite large structure can cause problems within the body including stroke like symptoms. Capillaries, which are small arteries, are about 8-10 microns, similar to a red blood cell in diameter. You can easily understand that such a large filament in enormous in size compared to capillaries.

There has been a lot of discussing regarding the rubbery clots and these filaments in the blood. The spike protein gene sequence shows that it produces Amyloid and Hydrogel, both can be used for biosensor technology:

Amyloid and Hydrogel Formation of a Peptide Sequence from a Coronavirus Spike Protein

Everybody Talks About Amyloid Or Prions In Relation To C19 Bioweapons. Review Of How Self Assembly Amyloid Hydrogels & Prion Peptides Are Used For Nanotechnology Devices & Biosensor Applications.

Study Shows ALL C19 Vaccinated Have Amyloid Microclots-Confirming 2022 Live Blood Study. Dissolution Of Amyloid Clots With EDTA, Vitamin C, Methylene Blue & DMSO - Successfully Done For Past 3 Years

Interestingly, in a nanotechnology study linked below, it shows that nanoparticles can accelerate the growth of Amyloid fibrils on surfaces - which the blood vessels in the body certainly have a lot of surface structure. Metallic nanoparticles have been used to accelerate the self assembly of Amyloid nano and microwires for electronic devices.

First, lets look at this microscopic video footage of active self assembly of a polymer filament in COVID19 unvaccinated blood. Magnification starts at 100x and goes up to 4000x. For best visualization of the moving nano and microparticles please enlarge the video window.

Here you can see further vesicles moving through the blood to arrive at the filament to contribute to self assembly:

The vesicles contain multicolored light emitting microrobots. These are the same I have filmed in deceased COVID19 vaccinated blood:

Zombie Blood - COVID19 Vaccinated Embalmed Blood For Over 2 Years Shows Continued Self Assembly Nanotechnology Replication, Nano and Microrobot Activity

In the video below you can see multiple small vesicles filled with nano and microrobots that are using the blood as an energy source to get to the filament and be part of the construction process. Adjacent to the filament you can clearly see how the vesicles elongated themselves to become denser and denser, and then are part of the long filament.

Below you can see 4000x magnification with Oil Objective. The particles in the vesicle clearly become part of the longer filament.

Here is what the nanotechnology literature discusses regarding Amyloid fibers that can be self assembled for electronic devices by using metal particles. This can explain why there were 55 undeclared semiconducting metals found in the COVID19 bioweapon injections.

Argentinian Heroic Scientists Are Persecuted For Their Research Of COVID19 Bioweapons & Finding 55 Undeclared Toxic Elements. Sign Petition NOW In Support Of Drs. Marcela Sangorin & Lorena Diblasi

The nanoparticles interaction with the molecules inside the body could be accelerating the Amyloid fibres production. Nanoparticles can be shedded from the COVID19 vaccinated or inhaled from Geoengineering, which uses the same chemical building blocks, namely toxic metals, Graphene and polymers.

Geoengineering Adverse Health Effects and Vaccine Nanoparticle Contaminations –

Discussion of the Common Thread of Toxic Heavy Metals and Graphene Oxide And their Removal with Intravenous EDTA Chelation in Clinical Practice

Remember Amyloid is used as a Hydrogel for Brain computer interface.

Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition

Abstract

Recent research in the field of nanometer-scale electronics has focused on the operating principles of small-scale devices and schemes to realize useful circuits. In contrast to established “top-down” fabrication techniques, molecular self-assembly is emerging as a “bottom-up” approach for fabricating nanostructured materials. Biological macromolecules, especially proteins, provide many valuable properties, but poor physical stability and poor electrical characteristics have prevented their direct use in electrical circuits. Here we describe the use of self-assembling amyloid protein fibers to construct nanowire elements. Self-assembly of a prion determinant from Saccharomyces cerevisiae, the N-terminal and middle region (NM) of Sup35p, produced 10-nm-wide protein fibers that were stable under a wide variety of harsh physical conditions. Their lengths could be roughly controlled by assembly conditions in the range of 60 nm to several hundred micrometers. A genetically modified NM variant that presents reactive, surface-accessible cysteine residues was used to covalently link NM fibers to colloidal gold particles. These fibers were placed across gold electrodes, and additional metal was deposited by highly specific chemical enhancement of the colloidal gold by reductive deposition of metallic silver and gold from salts. The resulting silver and gold wires were ≈100 nm wide. These biotemplated metal wires demonstrated the conductive properties of a solid metal wire, such as low resistance and ohmic behavior. With such materials it should be possible to harness the extraordinary diversity and specificity of protein functions to nanoscale electrical circuitry.

Here is the Amyloid fiber assembly with the small metal nanoparticles to create electrical circuitry:

Remember the electron Microscopy work by Dr Bremer showing razor like nanoparticles round these vesicles and in the COVID19 vaccinated blood.

Electron Microscopy Of The Blood Of A 43 Year Old With 3 Pfizer Injections Shows Nano Razors From Dr Hortencia Bremer

Image courtesy: Dr Hortencia Bremer, Electron Microscopy of nanorazors in COVID19 vaccinated blood.

It appears that Nanoparticles ACCELERATE the process of self assembly Amyloid fibrils. Below you can see images of filament assembly in minutes from the nanotechnology literature - interesting that “Corona” Bioweapon creates Amyloid fibrils that form a “Corona”. This is a peptide layer around the metal nanoparticles:

Peptide Self-Assembly into Amyloid Fibrils at Hard and Soft Interfaces—From Corona Formation to Membrane Activity

Peptides and proteins are exposed to a variety of interfaces in a physiological
environment, such as cell membranes, protein nanoparticles (NPs), or
viruses. These interfaces have a signiﬁcant impact on the interaction,
self-assembly, and aggregation mechanisms of biomolecular systems. Peptide
self-assembly, particularly amyloid ﬁbril formation, is associated with a wide
range of functions; however, there is a link with neurodegenerative diseases,
such as Alzheimer’s disease. This review highlights how interfaces aﬀect
peptide structure and the kinetics of aggregation leading to ﬁbril formation. In
nature, many surfaces are nanostructures, such as liposomes, viruses, or
synthetic NPs. Once exposed to a biological medium, nanostructures are
coated with a corona, which then determines their activity. Both accelerating
and inhibiting eﬀects on peptide self-assembly have been observed. When
amyloid peptides adsorb to a surface, they typically concentrate locally, which
promotes aggregation into insoluble ﬁbrils. Starting from a combined
experimental and theoretical approach, models that allow for a better
understanding of peptide self-assembly near hard and soft matter interfaces
are introduced and reviewed. Research results from recent years are
presented and relationships between biological interfaces, such as
membranes and viruses, and amyloid ﬁbril formation are proposed.

Figure 8. The condensation-ordering mechanism (COM) describes the acceleration of amyloid ﬁbril formation by NPs. Based on the nucleated conformational conversion model (NCC), nanoparticles accelerate the formation of unstructured oligomers and their conformational transition into 𝛽-sheet rich structures. Reproduced with permission. [39] Copyright 2018, The Royal Society of Chemistry

Such molecules are used in biotechnology including biosensing applications:

Bio-inspired amyloid polypeptides: From self-assembly to nanostructure design and biotechnological applications

The influence of thermodynamic and kinetic factors on the self-assembly of amyloid polypeptides are highlighted.
The evolution and current status of amyloid peptide-based nanomaterials on multiple dimensions are discussed.
The extension of applications ranging from biosensing, bioimaging, drug/gene delivery, cellular scaffolds and air pollution governance of amyloid polypeptide-based nanomaterials is shown.
The prospects and challenges of amyloid peptide-based nanomaterials are addressed.