Morgellons : The Breaking of Bonds and the Reduction of Iron
Biochemistry, BioEngineering, Chemistry, Health, Spectrometry

Morgellons : The Breaking of Bonds and the Reduction of Iron

Three methods that appear to interfere with the molecular bonding of the iron-dipeptide complex that is now understood to be characteristic of the "Morgellons" growth structure have been established and identified. The iron-protein complex is believed to be of, or similar to, the "Rieske Protein" (iron-sulfur) form. These three methods also appear to be variably successful in reducing the oxidation state of the encapsulated iron from the Fe(III) state to the Fe(II) state. The discovered methods involve the use of ascorbic acid (Vitamin C), N-acetyl cysteine (NAC) and glutathione. The results of applying glutathione appear to be especially promising at this time, as it appears that a major disruption in the bond structure has taken place after approximately 72 hours. The methods have been established and verified through visual, chemical and spectroscopic methods and each has an effect independent of the others. The hypothesis to be made here is that the growth of the organism itself may be interfered with as a result of this work.
MORGELLONS : A THESIS
Anomalies, Biochemistry, BioEngineering, Chemistry, Electrochemistry, Foundational, Health, Microbiology, Social & Political Impacts - Agencies - Media

MORGELLONS : A THESIS

Substantial evidence exists which proves not only the existence and presence of the "Morgellons" pathogen, but also how this organism uses iron from our blood for its proliferation and growth. This pathogen changes the iron in our blood from its ferrous form (Fe2+) to a ferric form(Fe3+). This change has a direct, negative impact on human health. The iron in human blood must be in the ferrous form in order for it to bind to the oxygen molecule. If our blood is not in this state then it will not bind to the oxygen molecule and human health will suffer. Proposed mitigation strategies are discussed.