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首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Exploring Hydrophobic Subdomain HA of the Protein Bovine Serum Albumin in the Native, Intermediate, Unfolded, and Refolded States by a Small Fluorescence Molecular Reporter
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Exploring Hydrophobic Subdomain HA of the Protein Bovine Serum Albumin in the Native, Intermediate, Unfolded, and Refolded States by a Small Fluorescence Molecular Reporter

机译：用小荧光分子报道分子探索天然，中间，未折叠和重新折叠状态的蛋白牛血清白蛋白的疏水亚域HA

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摘要

A simple intramolecular charge transfer (ICT) compound, 5-(4-dimethylamino-phenyl)-penta-2,4-dienoic acid methyl ester (DPDAME), has been documented to be a potential molecular reporter for probing microhet-erogeneous environments of a model transport protein bovine serum albumin (BSA) using spectroscopic techniques. Meteoric modifications to the emission profile of DPDAME upon addition of BSA come out to be a result of its binding to hydrophobic subdomain ETA. The highly polarity-sensitive ICT emission of DPDAME is found to be a proficient extrinsic molecular reporter for efficient mapping of native, intermediate, unfolded, and refolded states of the protein. Experimental data coupled with a reinforcing support from theoretical simulation using CHARMM22 software confirm the binding site of the probe to be the subdomain IIA of BSA, while FRET study reveals a remarkably close approach of our extrinsic molecular reporter to Trp-212 (in domain IIA): the distance between DPDAME and Trp-212 is 1.437 nm. The caliber of DPDAME as an external fluorescence marker also extends to the depiction of protein-surfactant (BSA-SDS) interaction to commendable fruition. Additionally, the protective action of small amounts of SDS on urea-denatured protein is documented by polarity-sensitive ICT emission of the probe. The present study also reflects the enhancement of the stability of BSA with respect to chemically induced denaturation by urea as a result of binding to the probe DPDAME.
机译：一个简单的分子内电荷转移（ICT）化合物5-（4-二甲基氨基-苯基）-戊-2,4-二烯酸甲酯（DPDAME）已被证明是潜在的分子报告子，可用于探测微异源环境使用光谱技术的模型运输蛋白牛血清白蛋白（BSA）。添加BSA后，对DPDAME发射曲线的流星雨修饰是由于其与疏水性亚结构域ETA结合的结果。发现DPDAME的高度极性敏感ICT发射是一种熟练的外在分子报告分子，可有效地绘制蛋白质的天然，中间，未折叠和重新折叠状态。实验数据加上使用CHARMM22软件进行理论模拟得到的加强支持，证实了探针的结合位点是BSA的IIA亚结构域，而FRET研究表明，我们的外在分子报道分子非常接近Trp-212（在IIA结构域中） ：DPDAME和Trp-212之间的距离是1.437 nm。作为外部荧光标记的DPDAME的口径还延伸到蛋白质表面活性剂（BSA-SDS）相互作用的描述，以取得可喜的成果。此外，探针对极性敏感的ICT发射记录了少量SDS对尿素变性蛋白的保护作用。本研究还反映了由于与探针DPDAME结合而导致的BSA在尿素化学诱导变性方面的稳定性增强。

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