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Bio Terrorism Solutions

Dynamic Adsorbents, Inc. Bio Terrorism Solution Dyna-CidalTM Description

Dyna-CidalTM is a solution of a special DAI proprietary compounds combined with a specially transformed particle of DAI Alumina. These unique positive and negative charges blanket the targeted contaminate. This material is very powerful in killing and capturing various microbes (bacteria and viruses) as well as bio terror toxins. Dyna-CidalTM is totally harmless, non flammable, and non toxic.

VX Capture Mechanism

Reactions with organophosphates and DAI alumina consist of nucleophilic relationships between the oxygen (or hydroxyl group) of the aluminum atoms and the phosphorous of the VX gas. Basically the positive charge (+) of the highly oxidized phosphorus attracts the negative charge of the oxygen or hydroxyl group. Post departure the aluminum of the alumina molecule will return to a positive state thus attracting the sulfur attached to the tertiary imines. This reaction not only eliminates VX gas by division of the molecule, but also traps the divided sections within the matrix of the DAI alumina layer.

Sarin Capture Mechanism

This is another interaction of organophosphates and the nucleophilic DAI alumina molecule. The bond between the phosphorus and the fluorine is slightly weak due to the natural state of the phosphorus being negative, but is acting positive due to the oxidation state it is in; fluorine gladly jumps ship for a positively charged hydrogen atom stolen off the surface of the DAI alumina. Once the fluorine has left the now negatively charged oxygen on the alumina surface pulls in the phosphorus. The “Sarin” has now been de-fluorinated; as well as, bound to the DAI alumina surface via a covalent bond. Further possible reactions are cleavage of the isopropyl group to form isopropynol after hydrolysis from moisture captured within the matrix of the DAI alumina and Dyna-CidalTM complex. This further detoxifies the Sarin.

Ricin Denature Mechanism

The association of DAI’s Dyna-CidalTM and the protein responsible for the toxic affect of “Ricin” is very complicated, far greater than can be explain here; the basics are as follows: The two strands of peptides composing the “Ricin” molecule are held together by a single di-sulfide bond. The protein is inadequate for toxic affect if both strands are not absorbed together. The beta-strand is the key to get the alpha-strand inside the cell. Our approach uses DAI Special to denature the protein then reducing the di-sulfide bond effectively cutting the molecule in half and capping the sulfur atoms off with hydrogen’s from the alumina surface. A typical DAI special aluminum oxide is in active state Brochmann level one which allows for a generous supply of hydrogen’s or hydroxide ions.

Ricin is poisonous if inhaled, injected, or ingested; it acts as a toxin by inhibiting protein synthesis. It prevents cells from assembling various amino acids into proteins according to the messages it receives from messenger RNA in a process conducted by the cell’s ribosome (the protein-making machinery)–that is, the most basic level of cell metabolism, essential to all living cells and thus to life itself. Ricin is resistant, but not impervious, to digestion by peptidases. By ingestion, the pathology of ricin is largely restricted to the gastrointestinal tract, where it may cause mucosal injuries; with appropriate treatment, most patients will make a full recovery.