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Modelisation of the Association Mechanism of a Series of Huperzine Derivatives Used for Alzheimer Disease with Human Serum Albumin: Effect of the Magnesium Cation

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Abstract

The role of the Mg2+ cation on huperzine molecule binding (drugs used for Alzheimer disease) on human serum albumin (HSA) was studied by affinity chromatography. The thermodynamic data corresponding to this binding were determined for a wide range of Mg2+ concentrations (x). For each solute, the huperzine binding on HSA was divided into two Mg2+ concentration regions. For a low x value, below x c (1.2 mM), the binding decrease with x. For x above x c the hydrophobic effect and van der Waals interactions between the huperzine molecule and the HSA implied a decrease in its binding. These results showed that for patients with Alzheimer disease, an Mg2+ supplementation during treatment with these huperzine molecules can increase the active pharmacological molecule concentration.

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Correspondence to Y. C. Guillaume.

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Morel, M., Thomassin, M., Berthelot, A. et al. Modelisation of the Association Mechanism of a Series of Huperzine Derivatives Used for Alzheimer Disease with Human Serum Albumin: Effect of the Magnesium Cation. Chroma 61, 253–258 (2005). https://doi.org/10.1365/s10337-005-0498-7

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  • DOI: https://doi.org/10.1365/s10337-005-0498-7

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