Copper Mediated Affinity of Amyloid β to Chondroitin Sulfates

b-Amyloid (Ab) is a major component of the senile plaques characteristic of Alzheimer disease (AD). Chondroitin sulfate (CS) and glycoaminoglycan (GAG) are also localized throughout the senile plaques in AD. In previous studies, the interaction of the Ab protein with CS immobilized on a chromatographic support and the role of aluminum and copper cations was studied using a molecular chromatographic approach [1,2]. Here, we demonstrated the direct implication of OHÁ radical formation on this binding via a novel analytical procedure. The binding of Ab amyloid on CS was accompanied by an OHÁ radical uptake. The Ab-CS complex was stabilized by the OHÁ radical via the creation of about one to two hydrogen bonds. The addition in the medium of a radical scavenger allowed decreasing the Ab/CS association and thus confirmed the positive role of these compounds in amyloidosis.

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OH· Radical Production Induces Direct Enhancement of the Amyloïd β Protein/Chondroitin Sulfate Binding: Inhibition by Potentially Radical Scavengers, a Biochromatographic and Thermodynamic Model

André¹,

Magy-Bertrand

Guillaume

2011

Chromatographia

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Copper Mediated Affinity of Amyloid β to Chondroitin Sulfates

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OH· Radical Production Induces Direct Enhancement of the Amyloïd β Protein/Chondroitin Sulfate Binding: Inhibition by Potentially Radical Scavengers, a Biochromatographic and Thermodynamic Model

OH· Radical Production Induces Direct Enhancement of the Amyloïd β Protein/Chondroitin Sulfate Binding: Inhibition by Potentially Radical Scavengers, a Biochromatographic and Thermodynamic Model

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