Bioactive anthraquinones found in plant foods interact with human serum albumin and inhibit the formation of advanced glycation endproducts

  • Weixi Liu
  • Ang Cai
  • Rachel Carley
  • Robert Rocchio
  • Zoe M. Petrovas
  • Cassie A. Chartier
  • Xiaofeng Meng
  • Jianyu Su
  • Bongsup P. Cho
  • Joel A. Dain
  • Hang Ma
  • Navindra P. Seeram


The glycation of human serum albumin (HSA) plays a critical role in the development of many disorders. Herein, the anti-glycation effects of several natural dietary anthraquinone derivatives including aloin, aloe-emodin, chrysophanol, emodin, physcion, and rhein were evaluated. The anthraquinones at 100 μM reduced fructose-, methylglyoxal-, and glyoxal-induced HSA glycation by 21% (aloe-emodin) to 92% (aloin), 17% (physcion) to 94% (emodin), and 16% (anthraquinone) to 67% (emodin), respectively. These anthraquinone derivatives also protected HSA by maintaining its free amino acid residues and secondary protein structure as characterized by circular dichroism. The mechanisms of their anti-glycation effects were investigated using rhein as a representative anthraquinone. The interactions between rhein and HSA were evaluated by biophysical characterizations, namely, isothermal titration calorimetry and UV-vis spectroscopy as well as computational modeling. Our findings suggest that the anti-glycation effects of these anthraquinones may be attributed to their binding capacity and stabilization of the HSA protein structure.


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