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Dietary anthocyanin–human serum albumin interaction

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Dietary anthocyanins occurring with different chemical structures are claimed to be beneficial for human health. The bioavailability of anthocyanins is the key factor influencing their health benefits. Fluorescence quenching method… Click to show full abstract

Dietary anthocyanins occurring with different chemical structures are claimed to be beneficial for human health. The bioavailability of anthocyanins is the key factor influencing their health benefits. Fluorescence quenching method was applied to determine the binding affinities of anthocyanins for human serum albumin. Demethylation of the methoxyl groups in anthocyanins enhanced the binding affinities. The number and position of the hydroxyl groups on ring [B] affect the affinities of anthocyanins for human serum albumin. The glycosylation of hydroxyl groups on ring [C] enhanced their binding affinities for human serum albumin. Anthocyanidins and anthocyanins, show different characteristics for their binding to human serum albumin when the methoxyl groups on the ring B are demethylated or hydroxylated.

Keywords: human serum; groups ring; binding affinities; serum albumin

Journal Title: Free Radical Biology and Medicine
Year Published: 2017

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