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Tea polyphenols bind serum albumins:A potential application for polyphenol delivery
Food Hydrocolloids ( IF 10.7 ) Pub Date : 2019-04-01 , DOI: 10.1016/j.foodhyd.2018.11.008
P. Chanphai , H.A. Tajmir-Riahi

Abstract Serum proteins play an important role as drug delivery in the clinical applications. We have determined the binding efficacy of tea catechins (+)-catechin (C), (−)-epicatechin gallate (ECG) and (−)-epigallocatechin gallate (EGCG) with human serum albumin (HSA) and bovine serum albumin (BSA) in aqueous solution at physiological pH. Thermodynamic parameters ΔH0 −13 to −8 (kJ mol−1), ΔS0 18 to 9 (J mol−1K−1) and ΔG0 -14 to −13 (kJ mol−1) showed tea catechins bind serum proteins via ionic interactions. The binding efficacy was 40–65% for polyphenol-protein conjugates. Modeling showed the presence of H-bonding, stabilizing catechin-protein conjugation with the free binding energy of −10.65 to −8.81 kcal/mol for catechin-HSA and −9.94 to −9.74 kcal/mol for catechin-BSA conjugates. Catechin conjugation induced major perturbations of the protein conformation. Our studies indicate that serum proteins can transport tea catechins in vitro.

中文翻译:

茶多酚结合血清白蛋白:多酚传递的潜在应用

摘要 血清蛋白在临床应用中作为药物传递发挥着重要作用。我们已经确定了茶儿茶素 (+)-儿茶素 (C)、(-)-表儿茶素没食子酸酯 (ECG) 和 (-)-表没食子儿茶素没食子酸酯 (EGCG) 与人血清白蛋白 (HSA) 和牛血清白蛋白 (BSA) 的结合功效) 在生理 pH 值的水溶液中。热力学参数ΔH0 -13 至-8 (kJ mol-1)、ΔS0 18 至9 (J mol-1K-1) 和ΔG0 -14 至-13 (kJ mol-1) 表明茶儿茶素通过离子相互作用与血清蛋白结合。多酚-蛋白质偶联物的结合效率为 40-65%。建模显示存在氢键,稳定儿茶素-蛋白质缀合,儿茶素-HSA 的自由结合能为 -10.65 至 -8.81 kcal/mol,儿茶素-BSA 偶联物的自由结合能为 -9.94 至 -9.74 kcal/mol。儿茶素结合引起蛋白质构象的主要扰动。我们的研究表明,血清蛋白可以在体外转运茶儿茶素。
更新日期:2019-04-01
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