An investigation of folic acid-protein association sites and the effect of this association on folic acid self-assembly
An investigation of folic acid-protein association sites and the effect of this association on folic acid self-assembly
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DOI：
10.1007/s00894-015-2847-2
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发表时间：
2015-12-01
影响因子：
2.2
通讯作者：
Mohanty, Sanat
中科院分区：
文献类型：
--
作者：
Gupta, Rajat;Kalita, Prasanta;Mohanty, Sanat
在使用 FA 作为蛋白质递送系统中的药物载体的背景下，研究了叶酸 (FA)-色氨酸相互作用对 FA-蛋白质关联的贡献。研究中使用牛血清白蛋白（BSA）和吲哚西丁作为模型蛋白。使用 Bradford 试剂对 FA-BSA 复合物进行表征，以确定 FA-BSA 结合对 BSA-染料试剂相互作用的影响。 FA-BSA 混合物的紫外可见光谱分析表明，即使 FA 与 BSA 结合后，BSA 染料试剂的最大吸光度也出现在 595 nm 处。这证实了蛋白质的质子化氨基酸基团不参与 FA-BSA 缔合。此外，分子动力学 (MD) 模拟证实了 FA 中的芳香族部分与吲哚西丁分子中的色氨酸部分之间存在缔合相互作用，从而破坏了 FA 自组装。 X 射线衍射 (XRD) 研究表明，添加 BSA 或色氨酸后，FA 自组装的破坏有限。这表明 FA 和 BSA 是相容且相互关联的。
The contribution of folic acid (FA)-tryptophan interactions to FA-protein association was investigated in the context of using FA as a drug carrier in protein delivery systems. Bovine serum albumin (BSA) and indolicidin were used as model proteins in the study. The FA-BSA complex was characterized by using the Bradford reagent to identify the impact of FA-BSA association on BSA-dye reagent interactions. UV-visible spectroscopic analysis of the FA-BSA mixture showed that the absorbance maximum of BSA-dye reagent occurred at 595 nm, even after the association of FA with BSA. This confirms that protonated amino acid groups of the protein are not involved in FA-BSA association. Moreover, molecular dynamics (MD) simulation confirmed the presence of an associative interaction between aromatic moieties in FA and tryptophan moieties in the indolicidin molecule, which disrupted FA self-assembly. An X-ray diffraction (XRD) study showed that there was limited disruption of FA self-assembly after the addition of BSA or tryptophan. This suggests that FA and BSA are compatible and associate with each other.