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Design, Synthesis and Spectroscopic Studies of Resveratrol Aliphatic Acid Ligands of Human Serum Albumin by Yu Lin Jiang is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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As one of the natural polyphenols, resveratrol possesses hydroxyl substituted trans-stilbene structure and exerts impact on health by inhibiting multiple human enzymes, such as cyclooxygenase, F1 ATPase, and tyrosinase. Resveratrol has to be bound by human serum albumin (HSA) to keep a high concentration in serum, since its solubility is low in water. To improve water solubility and bioavailability, two resveratrol aliphatic acids and their esters have been designed and synthesized. The solubilities of the resveratrol and its derivatives have been measured using a standard procedure. The two aliphatic acids showed better solubilities in pure water and phosphate buffer (pH 7). The binding affinities of resveratrol derivatives for HSA were also measured, and the drug-protein interaction mechanism was investigated using fluorescence, UV-vis, and NMR spectroscopies. Interestingly, resveratrol hexanoic acid (5) was found to be a much better ligand (K a = (6.70 ± 0.10) Â 10 6 M À1 ) for HSA than resveratrol (K a = (1.64 ± 0.07) Â 10 5 M À1 ), and there was 41-fold improvement for the binding affinity. It was the first time that the increase of fluorescence of resveratrol moiety was obser

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Author

Yu Lin Jiang

Publisher

Elsevier Science; Elsevier ; Elsevier Ltd.; Elsevier BV (ISSN 0968-0896)

Published

2008

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)