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Chromatographia

, Volume 61, Issue 5–6, pp 253–258 | Cite as

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

  • M. Morel
  • M. Thomassin
  • A. Berthelot
  • Y. C. Guillaume
  • C. André
Article

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.

Keywords

Column liquid chromatography Affinity chromatography Magnesium cation in human serum albumin Huperzine Alzheimer’s disease 

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Copyright information

© Friedr. Vieweg&Sohn/GWV Fachverlage GmbH 2005

Authors and Affiliations

  • M. Morel
    • 1
  • M. Thomassin
    • 1
  • A. Berthelot
    • 2
  • Y. C. Guillaume
    • 1
  • C. André
    • 1
  1. 1.Equipe des Sciences Séparatives et Biopharmaceutiques (2SB/EA482), Faculté de Médecine et de PharmacieBesançon cedexFrance
  2. 2.Equipe Optimisation du Métabolisme Cellulaire (OMC), Faculté de Médecine et de PharmacieBesançon cedexFrance

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