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Inhibition of Nonenzymatic Protein Glycation by Pomegranate and Other Fruit Juices

The nonenzymatic glycation of proteins and the formation of advanced glycation endproducts in diabetes leads to the crosslinking of proteins and disease complications.

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Our study sought to demonstrate the effect of commonly consumed juices (pomegranate, cranberry, black cherry, pineapple, apple, and Concord grape) on the fructose-mediated glycation of albumin.

RESEACH TITLE:  Inhibition of Nonenzymatic Protein Glycation by Pomegranate and Other Fruit Juices

COUNTRY: USA

CONDUCTED BY: Department of Pharmaceutical and Biomedical Sciences, College of Pharmacy, University of Georgia , Athens, Georgia, USA

PUBLISHED ON: Journal of Medicinal Food

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RESEACH: The nonenzymatic glycation of proteins and the formation of advanced glycation endproducts in diabetes leads to the crosslinking of proteins and disease complications. Our study sought to demonstrate the effect of commonly consumed juices (pomegranate, cranberry, black cherry, pineapple, apple, and Concord grape) on the fructose-mediated glycation of albumin. Albumin glycation decreased by 98% in the presence of 10 μL of pomegranate juice/mL; other juices inhibited glycation by only 20%. Pomegranate juice produced the greatest inhibition on protein glycation when incubated at both the same phenolic concentration and the same antioxidant potential. Both punicalagin and ellagic acid significantly inhibited the glycation of albumin by ~90% at 5 μg/mL. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that pomegranate, but not apple juice, protected albumin from modification. These results demonstrate that pomegranate juice and two of its major constituents are potent inhibitors of fructose-mediated protein glycation.

YEAR: 2014

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