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JOURNAL ARTICLE

Thiamin and protein folding

Derrick Lonsdale
Medical Hypotheses 2019, 129: 109252
31371089
A huge number of proteins that occur in the body have to be folded into a specific shape in order to become functional. Proteins are made up of chains of amino acids and the folding process is exquisitely complex. When this folding process is inhibited, the respective protein is referred to as being misfolded and nonfunctional. So the hypothesis that follows is in regard to the diseases that are caused by the misfolding of vital proteins and their reported relationship with thiamin metabolism. These diseases are termed proteopathies and there are at least 50 different conditions in which the mechanism is importantly related to a misfolded protein. In the brain, thiamin deficiency causes a cascade of events involving mild impairment of oxidative metabolism, neuroinflammation and neurodegeneration, including the pathology of Alzheimer's disease, Parkinson's and Huntington's diseases, all of which are examples of proteopathies. Prion diseases are fatal neurodegenerative disorders related to the conformational alteration of the prion protein (PrP C) into a pathogenic and protease-resistant isoform (PrPSc). The physiological form (PrP C) is a cell surface glycoprotein expressed mainly in the central nervous system. Despite numerous efforts to elucidate its role, the exact biological function remains unknown. Prion-induced diseases, due to the conformational change in the protein, are a global health problem, with lack of effective therapy and 100% mortality. Thiamin and its derivatives bind the prion protein and intermolecular actions have been noted between thiamin and other thiamin-binding proteins, although the exact importance of this is conjectural.

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