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Spectroscopic Techniques

Thimerosal changes protein conformation and increase the rate of fibrillation in physiological conditions: Spectroscopic studies using bovine serum albumin (BSA)
Published: 2018
SYNOPSIS

Thimerosal contributes to the formation of abnormal proteins associated with Alzheimer’s and other diseases.

CITATION

Santos JCN, da Silva IM, Braga TC, de Fátima Å, Figueiredo IM, Santos JCC. Thimerosal changes protein conformation and increase the rate of fibrillation in physiological conditions: Spectroscopic studies using bovine serum albumin (BSA). International Journal of Biological Macromolecules. 2018;113:1032-1040.

SUMMARY

A series of experiments suggests that the effects of the vaccine preservative thimerosal on the structure of important protein molecules in the blood are one likely cause of thimerosal’s toxicity, contributing to the development of neurodegenerative and other diseases. Using a cow protein as a proxy to assess thimerosal’s impact on human serum albumin (a protein made by the liver), the study found that thimerosal accelerates the build-up of abnormal protein deposits that are associated with at least 25 diseases, including Alzheimer’s, Parkinson’s and type 2 diabetes. When bound to albumin, thimerosal also may result in “more efficient distribution” of mercury in the body.

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