Press Releases Wed, 19 Jan 2022

COVID-19: Virus-Attenuate device now in Ghana market

SHYCOCAN™ ( The Scalene Hypercharge Corona Canon) is a unique device to ATTENUATE the Corona Family Viruses. It is designed for indoor purposes. The Device has undergone various efficacy tests in several international virology labs.

Various tests show that the Virus’s transmission mechanism is destroyed by the Shycocan and the Shycocan is hence referred to as Virus Attenuation Device. The device has been approved by the European CE and is manufactured and marketed under the U.S. FDA’s Enforcement Discretion Policy during a public health emergency.

It is also effective against SARS COV2, Influenza, and Swine Flu strains of Viruses. A recent White Paper Titled “WHY WILL SHYCOCAN CONTINUE TO BE A MASS PROTECTION FOR CORONA VIRUS INCLUDING B.1.1.529.1 (Omicron), B.1.640.1 (IHU) and Other Future Variants of Concern.” published by the Scientist States that “it (Shycocan) can be suitable for application to other mutations in S-protein including the Omicron (B.1.1.529.1) and future variants.”

The Shycocan is now also approved by Ghana GSA and Ghana FDA. The Shycocan can be switched on 24x7 in any enclosed public space to prevent the spread of the Corona Virus and it consumes as little power as a 40watt bulb. The Shycocan has undergone several tests for safety and has been proven to be safe for humans and pets.

The Device does not use any Ultra Violet rays, it does not emit any Ozone, and is considered more effective and safer than ionizers or Ozone based cleaners, or air purifiers. The Shycocan is already in use in several hospitals, schools, universities, offices, shops and many other such public spaces the world over. While we are still trying to get many to vaccinate, the Shycocan will strengthen our fight against Corona, and also help businesses get back to normal.


Scientific White Paper - Shycocan-variants of concern; CARD-022101; January 7,2022; Rel:1.10

Why will Shycocan continue to be mass protection for corona virus including b.1.1.529.1 (Omicron), b.1.640.1 (IHU), and other future variants of concern?

Rajah Vijay Kumar. D.Sc., Vishaka VK Pillai, MS (Regenerative Medicine)., Meena Augustus, PhD., Centre for Advanced Research and Development (CARD), Organization de Scalene Foundation, India.

The newly reported Omicron variant is poised as the most rapidly spreading SARS-CoV-2 variant across the world. Cryo-EM structural analysis of the Omicron variant spike protein (fig.1) in complex with human ACE2 reveals new salt bridges and hydrogen bonds formed by mutated residues R493, S496, and R498 in the RBD with ACE2.

These interactions appear to compensate for other Omicron mutations such as K417N known to reduce ACE2 binding affinity, explaining similar biochemical ACE2 binding affinities for Delta and Omicron variants. The retention of strong interactions at the ACE2 interface and the increase in antibody evasion are molecular factors that likely contribute to the increased transmissibility of the Omicron variant.

Figure 1. Cryo-EM structure of the Omicron spike protein. (A)

A schematic diagram illustrating the domain arrangement of the spike protein. Mutations present in the Omicron variant spike protein are labeled. (B) Cryo-EM map of the Omicron spike protein at 2.79 Å. Protomers are colored in shades of purple. (C) Cryo-EM structure of Omicron spike protein indicates the locations of all mutations on one protomer. (D) The Omicron spike receptor-binding domain (RBD) is shown in two orthogonal orientations. Cα of all mutated residues are shown as red spheres [1].

The Omicron (B.1.1.529.1) variant, first reported on November 24, 2021, was quickly identified as a variant of concern (VoC) with the potential to spread rapidly across the world. There is widespread concern about the speed with which the Omicron variant is currently circulating even amongst doubly vaccinated individuals. The Omicron variant spike protein has 3-5 times more mutations than that seen in any of the previous SARS-CoV-2 strains.

The question is will Nano electric field caused by Photon Mediated Electron Emission (PMEE) or other methods, be able to interact with the ACE2-S-Protein binding mechanism of the highly mutated Omicron VOC. Understanding the consequences of these mutations for ACE2 receptor binding and neutralizing antibody evasion is important in assessing the action of Scalene Hypercharge Corona Canon (SHYCOCAN) in attenuating or neutralizing the S-Protein receptor binding domine of the Omicron variant of the SARS-COV-2 virus for effectively limiting the spread of the Omicron and related variants.

An Interesting Independent study was done by Martin E.

Garcia et.al at the Theoretical Physics and Centre for Nanostructure Science and Technology, Universität Kassel, Germany, on the vulnerability of electronic fields on SARS-CoV-2 spike protein with the help of atomistic simulations. A paper titled “SARS-CoV-2 Spike protein is vulnerable to moderate electric fields” was recently published in Nature Communications [Nature Communications | (2021)2:5407| http://doi.org/10.1038/s41467-021-25478-7 |

www.nature.com/naturecommunications.] The binding of the spike protein with the ACE2 receptor of the host cell constitutes the first and key step for virus entry into host cells. During this process, the receptor-binding domain (RBD) of the S protein plays an essential role, since it contains the receptor-binding motif (RBM), responsible for the docking to the receptor.

So far, mostly biochemical methods are being tested to prevent the binding of the virus to ACE2. It has been shown, with the help of atomistic simulations, that external electric (electron) fields (EF) of the wide spectrum and moderate strengths can dramatically destabilize the S protein, inducing long-lasting structural (attenuation) damage.


SHYCOCAN Mechanism of action on the S-Protein of the Viral Particle.

The effect of wide spectrum moderate fields can be understood in terms of the interactions of these fields with the permanent dipoles located in the backbone structure and with the additional flexible dipoles on the protein side chains (see Fig. 3d).

For instance, under the action of an EF, the electric dipole moments can be reoriented along the field direction in order to minimize the electrostatic energy. On the other hand, a rearrangement of the dipoles can cost conformational energy due to the loss of hydrogen bonds.

As a result of the balance between conformational and electrostatic energies along with entropic contributions, the protein can undergo a significant conformational change [2]. It has been established that relatively low to moderate EFs can persistently change both the secondary and tertiary structures of S by rearranging and reorienting residues, thus disordering originally ordered segments through breaking and rebuilding of hydrogen bonds and salt bridges.

SHYCOCAN device produces EF in closed and open spaces and its efficacy has been tested a a number of laboratories of repute on the surface and Arial SARS

CoV-2 and another coronavirus.

SHYCOCAN is a mass protection virus defense technology of the future, here to stay.

External EF affect the attachment of SARS-Cov-2 to the host cell.

virus entry into the cell is mediated by the recognition between the spike glycoprotein (S protein) present in the virus envelope and the angiotensin-converting-enzyme receptor (ACE2) of the host cell membrane. The binding between the S protein and ACE2 can be altered when external EF induces drastic conformational changes and damage in the S protein.b Sequence of the S protein (PDB IDs: 6VSB and 6M0J1).

Highlighted in colors is the segment used in this study. c Conserved number of native contacts (NC) between residues of S and ACE2 for different magnitudes of the EF strength. NC is maximal for native S protein. Very strong electric fields(109 V/m) disable the protein by largely deforming its shape, leaving a structure that is unrecognized by ACE2 (NC = 0).

Moderate electric fields, which can be induced by SHYCOCAN, strongly reduce NC and are therefore candidates to decrease the affinity of S to ACE2 and, consequently, the infectivity of the virus. The best 6 matches (higher Nc) are taken for each condition for comparison. In the box-whisker plot, the centralline indicates median, box limits indicate upper and lower quartiles, and whiskers specify maxima and minima.

Source data are provided with this paper. d Changes in the structural conformation of proteins under EF are driven by the reorientation of electric dipoles. (NATURE COMMUNICATIONS | (2021) 12:5407 | https://doi.org/10.1038/s41467-021-25478-7 | www.nature.com/ )

Thus, at the sub-microsecond time scale, significant damage on the tertiary and secondary structure of the S protein affects its interaction with ACE2, potentially making SARS-Cov-2 less infectious.

These results pave the way to a range of possible applications of EFs to control structural changes in virions with SARS-CoV-2 being one of the multiple targets.

An Important EF-induced conformational change occurs at the level of the recognition loop L3 of the RBD where two parallel beta-sheets, believed to be responsible for a high affinity to ACE2, undergo a change into an unstructured coil, which exhibits almost no binding possibilities to the ACE2 receptor.

It is also shown that these severe structural changes upon EF exposure also occur in the mutant RBDs corresponding to the variants of concern (VoC) B.1.1.7 (UK), B.1.351 (South Africa), and P.1 (Brazil). Remarkably, while the structural flexibility of S allows the virus to improve its probability of entering the cell, it is also the origin of the EF-induced vulnerability of S upon application of EF of strengths at least two orders of magnitude smaller than those required for damaging most proteins.

The study [2] has found the existence of a clean physical process to weaken the SARS-CoV-2 virus without further biochemical processing. Moreover, the effect could be used for infection prevention purposes and to also develop technologies for in-vitro structural manipulation of S-protein. Since the process is

largely unspecific, it can be suitable for application to other mutations in S protein including the Omicron (B.1.1.529.1) and future variants.

The function of coronavirus spikes and their evolution through mutations, enhance our understanding of the origin of viruses and the evolutionary relationship between viruses and host cells [4].

Given that the Spike is an essential means to ensure the survival of coronaviruses mediating the binding to the human host cell receptor, offers a unique means for physical attenuation with the safe EF created by the release of free photon mediated electrons by the PMEEs, in real-time.


This is a scientific white paper to explain why SHYCOCAN, Virus Attenuation Device would be effective in cases of new VoC (Omicron – B.1.1.529.1, IHU - B.1.640.1), based on the scientific knowledge available today. This is not publicity or marketing material. This document is for educational purposes only.


1. Sriram Subramaniam et.al., SARS-CoV-2 Omicron Variant: ACE2 Binding, Cryo-EM Structure of Spike Protein-ACE2 Complex and Antibody Evasion;

https://doi.org/10.1101/2021.12.19.473380; December 21, 2021.

2. Martin E. Garcia et.al., SARS-CoV-2 Spike protein is vulnerable to moderate electric fields; Nature Communications | (2021)2:5407| http://doi.org/10.1038/s41467-021-25478-7 | www.nature.com/naturecommunications.

Scientific White Paper - Shycocan-variants of concern; CARD-022101; January 7,2022; Rel:1.10

3. Didier Raoult et.al., Emergence in Southern France of a new SARS-CoV-2 variant of probably Cameroonian origin harboring both substitutions N501Y and E484K in the spike protein; DOI: https://doi.org/10.1101/2021.12.24.21268174; December 29, 2021.

4. Fang Li., Structure, Function, and Evolution of Coronavirus Spike Proteins; Annu. Rev. Virol. 2016.3:237-261. www.annualreviews.org • Coronavirus Receptor Recognition and Cell Entry.

Contact: shycocan@pioneertransafricon.com: www.pioneertransafricon.com


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Source: Thiran Africa Limited
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