“The unregulated advancement of biotech is creating a new arms race and threatening our personal autonomy.” – Spartacus
A document posted online under the name “Spartacus” went viral in 2021. The ‘Covid letter’ summed up the state of the ‘pandemic’ at the time, calling out the so-called ‘science’ attributed to Covid-19 and the vaccines. Since then, Spartacus has written several documents including ‘Covid-19: A Web of Corruption’ and a four-part series ‘Covid-19: Deep Dive’.
Below is the latest article published by Spartacus, ‘The Weaponization of Biotech’:
“After our previous article on this topic, I was asked by someone off-site to cite specific examples of biotechnology that could be misused for nefarious purposes, or could have utility as clandestine military or intelligence tools. It was a fair criticism. I listed off a number of technologies that could have such uses, but did not cite any specific articles to make my case. This article will address that deficiency.”
We are publishing Spartacus’ this document in sections for those who struggle to find the time to read the paper in full in one sitting. This is the fifth in our series.
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In Vivo Biofabrication
With some new types of biotechnology, it may be possible to “print” novel structures inside the body using biological processes.
Take, for instance, Ehud Gazit’s research into the usage of repeating amyloid units to assemble artificial structures.
Self-assembled peptide and protein amyloid nanostructures have traditionally been considered only as pathological aggregates implicated in human neurodegenerative diseases. In more recent times, these nanostructures have found interesting applications as advanced materials in biomedicine, tissue engineering, renewable energy, environmental science, nanotechnology and material science, to name only a few fields. In all these applications, the final function depends on: (i) the specific mechanisms of protein aggregation, (ii) the hierarchical structure of the protein and peptide amyloids from the atomistic to mesoscopic length scales and (iii) the physical properties of the amyloids in the context of their surrounding environment (biological or artificial). In this review, we will discuss recent progress made in the field of functional and artificial amyloids and highlight connections between protein/peptide folding, unfolding and aggregation mechanisms, with the resulting amyloid structure and functionality. We also highlight current advances in the design and synthesis of amyloid-based biological and functional materials and identify new potential fields in which amyloid-based structures promise new breakthroughs.
In a further example, the formation of fibrils (so-called protein nanofibres) by the extracellular matrix (ECM) adhesion protein fibronectin was observed after incubation at 37 °C in water/ethanol mixtures.94 The fibrils were used as scaffolds to deposit N-hydroxysulfosuccinimide (NHS)-modified CdSe–ZnS core–shell quantum dots (QDs), which had potential applications as biophotonic nanohybrid materials. Fibrinogen also forms fibrils by incubation at pH 2, and these were used as templates for biomineralization.95
Recent studies have revealed that several natural protein aggregates possess intrinsic semiconductive optical properties (15). Kaminski et al. demonstrated that when excited at 405 nm, the assemblies of misfolded proteins associated with neurodegenerative disorders can exhibit intrinsic fluorescent emission (16, 17). This label-free autofluorescence allows quantitative assessment of the kinetics of amyloid fibrillar formations, eliminating the need for extrinsic labeling, which might result in steric hindrance and other perturbations during aggregation (16).
Self-assembled structures made of very short peptides, including fragments of such amyloidogenic proteins, may also have intriguing semiconductive properties because their band gaps are comparable to those of conventional materials (18). Furthermore, their bioderived nature and rigid self-assembly (19, 20) can minimize the potential cytotoxicity of the building blocks (21), demonstrating the biocompatibility of the supramolecular structures. Enantiomers determine the enzymatic sensitivity (l-type) or resistance (d-type) of self-assemblies (22), thus underlying their controllable biosustainability. Also, the weak reducibility of the amino acids implies the strong oxidation stability of the supramolecular structures (23). By virtue of their simple and low-cost synthesis, as well as their ease of modulation relative to their larger counterparts, these self-assembled peptide semiconductors may serve as candidates for advanced interdisciplinary functional nanostructures (24, 25).
If you could assemble semiconductors in people’s bodies out of amyloid in an ordered and regulated way, you could assemble the components of a literal biocomputer inside someone’s body.
It is an odd coincidence that SARS-CoV-2’s proteins are highly amyloidogenic.
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