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​The chemistry behind Airora

Bacteria, Viruses and Vegetative Spores (Mould)

Hydroxyl radicals (hydroxyls) are lethal to pathogenic viruses and bacteria (both gram –ve & +ve), for example Coronaviruses, MRSA, C.difficile, Salmonella, Norovirus, and Flu Virus, both in the air and on surfaces.

The cascade process created by Airora is a condensing process, in that it has zero vapour pressure, therefore viruses, bacteria, particles, other molecules and surfaces in general will be “coated” at a molecular level by the reactants, and the hydroxyl radicals yielded will oxidise the targets. 

In general terms hydroxyl radicals kill all types of bacteria and viruses as well as moulds by reacting with the lipids and proteins in their thin, delicate cell membranes, causing lysing (breakdown).

Pathogenic bacteria succumb to hydroxyl radicals because hydroxyls are extremely small (just one atom of hydrogen and one atom of oxygen), and able to pass through the outer cell wall structures of the bacteria where they can oxidise the third membrane responsible for electron transport. This membrane is highly sensitive to oxidation, and minor disruption will render the whole organism non-viable.

Pathogenic viruses suffer from oxidation of their surface structures. The hydroxyl radicals disrupt the lipid envelope and/or capsid (protein shell) around the virus and inactivate the protein used to enter human cells. Hydroxyl radicals also penetrate the interior of the virus and disrupt the genome (RNA/DNA content). These reactions inactivate the virus, rendering it completely harmless and unable to infect humans and animals.

Hydroxyl radicals are incredibly reactive and as the Airora process produces a never-ending supply, so even clumps of cells, thick layers and heavy cell walls (such as TB and spores) will eventually succumb. 

The process kills the target organisms in such a way as to maintain their antigen “signature” without viability, which means they can still induce 'passive immunity'.

Humans, animals, insects and even normal skin flora have evolved within an environment that is rich in hydroxyl radicals and are therefore immune to their actions.

Tests at the UK Government’s Health Protection Agency’s Centre for Emergency Preparedness & Response at Porton Down have shown that exposure to hydroxyl radicals created by our technology:

• Killed 99.9999% of airborne test virus  (MS2 Coliphage) in less than 5 minutes
• Killed 99.999% of airborne Staphylococcus epidermidis in less than 2 minutes
• Killed 99.9999% of surface concentration of MRSA on glass over a 24 hour period

​COVID-19 and MS2 Coliphage

While it is not possible at this time (for safety reasons) to test our technology directly against the COVID-19 virus, we know that Airora's technology destroys ALL types of pathogenic viruses, including those in the coronavirus family (which includes the SARS-CoV-2 coronavirus that causes COVID-19), in the air and on surfaces. 

This is demonstrated by the testing carried out by Public Health England's microbiologists at Porton Down using MS2 Coliphage as a surrogate. In every test, our process quickly rendered MS2 Coliphage inactive in the air and on surfaces.  

​The microbiologists at Porton Down use MS2 Coliphage as a gold-standard surrogate for pathogens because it is exceedingly difficult to inactivate. If you can use a process to inactivate MS2 Coliphage then that process would be expected to inactivate all types of pathogenic virus and bacteria. Like all coronaviruses, MS2 is a positive sense single-stranded RNA virus and studies have shown that it is 7 to 10 times more resistant to denaturation (i.e. harder to inactivate) than a coronavirus. ​​

As an example of how hydroxyls inactivate human coronaviruses, the following paper makes specific reference to the role of hydroxyls in inactivating coronaviruses on surfaces, in the same way as they kill other viruses:​

Read an example of hydroxyls inactivating human coronaviruses >

Allergens

​Allergens usually enter the respiratory system through the nose. Mast cells in the airways release mediators, which trigger the allergy attack. This attack is an overreaction of the body’s immune system to the invading allergens that have bonded with antibodies.  Mast cells are one of the human body’s principal defences against allergens and are found in connective tissue and mucous membranes. One of its biological functions is innate immunity including involvement in host defence mechanisms against parasitic infestations, tissue repair, etc.

Mast cells contain pockets of granules rich in histamine and heparin that cause allergy if triggered by invading allergens. In allergy sufferers Immunoglobulin E (IgE) antibodies present on the surface of mast cells trigger the release of histamine when allergens stick to these IgE antibodies. This irritates the mucous membrane in the upper airways, which manifests itself for example through coughs and sneezes.​
​Hydroxyl radicals have been shown to reduce IgE-binding capacity in pollens, spores and pet dander through the degradation and modification of the tertiary structure and/or the induction of protein denaturation and/or aggregation. This allergen structure is no longer recognised by the body's immune system and therefore histamine and other chemical mediators are not released.

​Pollens, Non Vegetative Spores and Pet Dander

​Hydroxyl radicals have been shown to modify the IgE-binding capacity in pollens, spores and pet dander through the degradation and modification of the tertiary structure and/or the induction of protein denaturation and/or aggregation. This modified allergen structure is no longer recognised by the body's immune system and therefore histamine and other chemical mediators are not released.

References:
While the references below refer in their titles to cluster ions, the text makes it clear that the recorded effects are achieved by hydroxyl radicals which result from the chemical interactions between the cluster ions.
  1. Kawamoto S et al. Decrease in the Allergenicity of Japanese Cedar Pollen Allergen by Treatment with Positive and Negative Cluster Ions, International Archive of Allergy and Immunology, 2006, Vol.141, No. 4
  2. Kazuo Nishikawa et al. Exposure to positively and negatively charged plasma cluster ions impairs IgE binding capacity of indoor cat and fungal allergens, World Allergy Organization Journal 2016​

​House Dust Mites

Hydroxyl radicals instantly denature the allergens Der p1 and Der f1 found in house dust.

Hydroxyls radicals oxidise their protein structures, for example causing protein backbone damage due primarily to a hydrogen atom abstraction at the alpha carbon. This process leads to backbone fragmentation.
​
Side-chain damage is another protein oxidation mechanism and can occur through hydrogen abstraction or oxygen addition. Both hydroxyl radical initiated oxidation mechanisms result in a modified allergen structure. This modified allergen structure is no longer recognised by the body's immune system and therefore histamine and other chemical mediators are not released.

References:
  1. Garrison W M. Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins. Chem Rev 1987:381-398 -9920.
  2. Singh J & Thornton J M. Atlas of Protein Side-Chain Interactions, Vols. I & II, 1992 IRL press, Oxford.

Ozone and Carbon Monoxide

Hydroxyl radicals have a strong tendency to remove (abstract) a hydrogen atom from organic species (RH) whenever possible. The organic radical (R) then reacts with oxygen (O2) to form organic peroxides (RO2).

On a global scale, OH reacts primarily with carbon monoxide (40%) to form carbon dioxide, around 30% of the OH produced is removed from the atmosphere in reactions with organic compounds and 15% reacts with methane (CH4). The remaining 15% reacts with ozone (O3), hydroperoxy radicals (HO2) and hydrogen gas (H2).

OH reacts with ozone according to the following reaction mechanism:
OH• + O3 → HO4•
HO4• → O2 + HO2•

OH reacts with CO according to the following reaction mechanism:
CO + OH• → CO2 + H

​Pollutants & Volatile Organic Compounds (VOCs)

​Including odours, Formaldehyde, Ammonia and Ultra-Fine Particles
​Hydroxyl radicals react within 20-60 milliseconds with VOCs and initiate a series of fast, free radical chain reactions that continuously decompose VOCs and their byproducts, keeping air safe to breath.

Hydroxyl radicals oxidise and decompose VOCs by a series of free radical chain reactions which are very fast and efficient – thousands of times faster than ionic reactions that characterise ionisation and plasma systems and a million times faster than ozone.

The cascade of secondary oxidants formed is more stable, and circulate throughout the treatment area to complete the purification process. Oxidant and byproduct concentrations are diluted to the safe levels found in nature, which range from 10-40 ppb.

Byproducts recirculate until they are fully oxidised – a process which “clips” off carbon atoms one at a time, forming carbon dioxide and water.

Smaller VOCs react more quickly, so oxidation byproducts like formaldehyde or acetaldehyde don’t accumulate.

Ultra-fine particles (less than 0.1 microns) are known to be potentially harmful to health, make up around 90% of all airborne particles and are too small to be captured by a HEPA filter. Typically, about a half of ultra-fine particles are particle-phase organic carbon. These organic carbon particles are subject to heterogeneous oxidation by the gas-phase hydroxyl radical. The amount of particle-phase carbon decreases with oxidation, due to fragmentation (C - C scission) reactions that form small, volatile products that escape to the gas-phase. 

Simply put, only Airora provides continuous whole-space protection

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  • Home
  • Products
    • Airora Professional
    • Airora Personal
  • The Science
    • The Amazing Science of Hydroxyls
    • The Problems With Filters, Foggers and UVC Disinfection
    • Imagined by NASA, Delivered by Airora
    • Compare Airora to Filter-Based Air Cleaning Technologies
    • The Chemistry Behind Airora
    • Scientific Testing & Verification
  • About Us
  • Newsroom
    • Blog
    • Media Resources
  • Contact