Interaction mode and nanoparticle formation of bovine serum albumin and anthocyanin in three buffer solutions
Interaction mode and nanoparticle formation of bovine serum albumin and anthocyanin in three buffer solutions
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牛血清白蛋白和花青素在三种缓冲溶液中的相互作用模式和纳米颗粒的形成
DOI：
10.1016/j.jlumin.2014.06.037
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发表时间：
2014-11
影响因子：
3.6
通讯作者：
Jing Hao
中科院分区：
文献类型：
--
作者：
Zhou Rui;Dong Xueyan;Song Lanlan;Jing Hao
研究不同溶液中牛血清白蛋白（BSA）和花青素（ACN）的相互作用模式将有助于我们了解生物活性小分子和生物大分子的相互作用机制和功能变化。本研究利用荧光光谱和同步荧光光谱研究了磷酸盐（PBS）、氯化钠（NaCl）和PBS-NaCl三种缓冲溶液中BSA与ACN相互作用的结合模式，包括结合常数、结合位点数量、结合力。还使用动态光散射 (DLS) 和透射电子显微镜 (TEM) 研究了 BSA-ACN 复合物的形成和特性。结果表明，ACN 可以通过氢键和范德华力与 BSA 的酪氨酸（Tyr）和色氨酸（Trp）残基相互作用，并且在 dH2O 和三种缓冲溶液中观察到相同的结合模式。随着温度从298 K升高到308 K，结合常数K值逐渐减小，其减小程度依次为dH2O（9.0×104）> NaCl（2.64×104）/PBS（2.37×104）> PBS-NaCl（0.88×104），且与缓冲液的离子强度呈负相关（PBS-NaCl> NaCl> PBS）。这表明 BSA-ACN 复合物的稳定性在 dH2O 中比在三种缓冲溶液中受到的影响最大。 BSA 和 ACN 相互作用导致 BSA-ACN 纳米颗粒的形成。 dH2O 中的 BSA-ACN 纳米粒子的尺寸小于三种缓冲溶液中的尺寸，这与室温（25°C，298K）下 dH2O 中的 BSA 和 ACN 之间的结合力强于三种缓冲溶液中的结合力相关。
Investigation of interaction mode of bovine serum albumin (BSA) and anthocyanin (ACN) in different solutions will help us understand the interaction mechanism and functional change of bioactive small molecule and biomacromolecule. This study investigated the binding mode, including binding constant, number of binding sites, binding force of BSA and ACN interaction in three buffer solutions of phosphate (PBS), sodium chloride (NaCl), and PBS-NaCl, using fluorescence spectroscopy and synchronous fluorescence spectroscopy. Formation and characteristics of BSA–ACN complex were also investigated using dynamic light scattering (DLS) and transmission electron microscopy (TEM). The results showed that ACN could interact with BSA at both tyrosine (Tyr) and tryptophan (Trp) residues through both hydrogen bonds and van der Waals force, and the same binding mode was seen in dH2O and three buffer solutions. The value of binding constantKwas decreased as the temperature increased from 298 K to 308 K, and the decreasing degree was in the order of dH2O (9.0×104)>NaCl (2.64×104)/PBS (2.37×104)>PBS-NaCl (0.88×104), which was inversely correlated with the ionic strength of the buffer solutions of PBS-NaCl>NaCl>PBS. It indicated that stability of BSA–ACN complex was affected most in dH2O than in three buffer solutions. The BSA and ACN interaction led to formation of BSA–ACN nanoparticles. The sizes of BSA–ACN nanoparticles in dH2O were smaller than that in three buffer solutions, which correlated with stronger binding force between BSA and ACN in dH2O than in three buffer solutions at room temperature (25 °C, 298 K).
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影响因子：
6.1
作者：
M. Yang;Yue Wu;Jinbing Li;Haibo Zhou;Xiaoyong Wang
通讯作者：
M. Yang;Yue Wu;Jinbing Li;Haibo Zhou;Xiaoyong Wang
DOI：
10.1016/s0141-8130(97)01159-8
发表时间：
1997-06-01
影响因子：
8.2
作者：
Giancola, C;DeSena, C;Barone, G
通讯作者：
Barone, G
影响因子：
3.6
作者：
Bi, Shuyun;Yan, Lili;Wang, Yu
通讯作者：
Wang, Yu
影响因子：
4.4
作者：
Liu, Yan;Chen, Mingmao;Song, Ling
通讯作者：
Song, Ling
影响因子：
14.5
作者：
Li, Yunfang;Yang, Guangzhong;Mei, Zhinan
通讯作者：
Mei, Zhinan