机构地区:[1]School of Chemical Engineering and Technology,Tianjin University [2]Medical Plant Lab,Tianjin Research Center of Agricultural Biotechnology
出 处:《Transactions of Tianjin University》2017年第4期325-333,共9页天津大学学报(英文版)
基 金:supported by the National Natural Science Foundation of China (No. 31,271,979 and No. 31,571,825);the Natural Science Foundation of Tianjin (No.15JCYBJC30100)
摘 要:Biochanin A (BCA), the most abundant isoflavone in chickpeas, presents a wide range of biological activities, such as hypolipidaemic, anti-oxidative, anti-proliferative, and estrogen-like effects. We investigated the interaction between BCA and human serum albumin (HSA) via several techniques. UV–Vis absorption spectroscopy verified the conformational variation of HSA after BCA addition, and fluorescence spectroscopy revealed the relevant binding parameters. Circular dichroism spectroscopy was used to estimate the secondary structural changes of HSA with and without BCA. Molecular docking and dynamics simulations were then applied to study the characteristics of HSA with BCA. Energy decomposition analysis was used to prove that Trp214 in subdomain IIA of HSA is the most likely binding site of BCA. Van der Waals forces and hydrophobic interactions may play important roles during the binding process. All of our results showed that BCA presents significant binding affinity to HSA, thus confirming that the role of HSA has as an efficient transporter of biomolecules. © 2017, Tianjin University and Springer-Verlag Berlin Heidelberg.Biochanin A(BCA), the most abundant isoflavone in chickpeas, presents a wide range of biological activities, such as hypolipidaemic, anti-oxidative, antiproliferative, and estrogen-like effects. We investigated the interaction between BCA and human serum albumin(HSA) via several techniques. UV–Vis absorption spectroscopy verified the conformational variation of HSA after BCA addition, and fluorescence spectroscopy revealed the relevant binding parameters. Circular dichroism spectroscopy was used to estimate the secondary structural changes of HSA with and without BCA. Molecular docking and dynamics simulations were then applied to study the characteristics of HSA with BCA. Energy decomposition analysis was used to prove that Trp214 in subdomain ⅡA of HSA is the most likely binding site of BCA. Van der Waals forces and hydrophobic interactions may play important roles during the binding process. All of our results showed that BCA presents significant binding affinity to HSA, thus confirming that the role of HSA has as an efficient transporter of biomolecules.
关 键 词:Absorption spectroscopy Binding energy Bins Body fluids DICHROISM FLAVONOIDS Fluorescence spectroscopy HYDROPHOBICITY Molecular biology Molecular dynamics Van der Waals forces
分 类 号:R151[医药卫生—营养与食品卫生学]
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