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研究新型合成金属表面活性剂存在下牛血清白蛋白的结构完整性。

Investigating the structural integrity of Bovine serum albumin in presence of newly synthesized metallosurfactants.

机构信息

Department of Chemistry and Centre of Advanced studies in Chemistry, Panjab University, Chandigarh, India.

Department of Chemistry and Centre of Advanced studies in Chemistry, Panjab University, Chandigarh, India.

出版信息

Colloids Surf B Biointerfaces. 2018 Apr 1;164:116-124. doi: 10.1016/j.colsurfb.2018.01.025. Epub 2018 Jan 31.

DOI:10.1016/j.colsurfb.2018.01.025
PMID:29413588
Abstract

Bovine Serum Albumin is major transport protein and is often used as a drug carrier in body organs. Knowledge of its binding with metallosurfactant can significantly influence the biodistribution of metallodrugs. Current work demonstrated a facile method to prepare four different double chained metallosurfactants containing Fe, Co, Ni and Cu as part of their counter ion. The as-synthesized metallosurfactants were characterized using FTIR, AAS, TGA and XRD in solid form. The aggregation of these metallosurfactants in aqueous medium was investigated through conductivity, surface tension and SAXS. Further, we have investigated their binding with BSA through different analytical methods The effect of concentration of metallosurfactants on the primary and secondary structure of BSA was further examined by SDS-PAGE and Circular dichroism, respetively. It is found that at premicellar concentration, the primary structure of BSA was not affected but the secondary structure i.e. α-helical structure of BSA was altered as shown by circular dichroism. Interestingly, post micellar concentration of metallosurfactants shows the pronounced effect on the primary and secondary structure of BSA. SAXS study also supports the fact of unfolding of protein and its wrapping around the micelles. Zeta potential describes the electrical charge and stability of the protein in the presence of different concentration of metallosurfactant. Along with, it was found that presence of protein delays the aggregation behavior of metallosurfactant, as a sign of binding of BSA with metallosurfactant.

摘要

牛血清白蛋白是主要的转运蛋白,常被用作药物载体在体内器官。了解其与金属表面活性剂的结合可以显著影响金属药物的生物分布。目前的工作展示了一种简便的方法来制备四种不同的双链金属表面活性剂,它们的反离子部分含有 Fe、Co、Ni 和 Cu。合成的金属表面活性剂在固态下通过 FTIR、AAS、TGA 和 XRD 进行了表征。通过电导率、表面张力和 SAXS 研究了这些金属表面活性剂在水介质中的聚集情况。此外,我们通过不同的分析方法研究了它们与 BSA 的结合。通过 SDS-PAGE 和圆二色性分别进一步研究了金属表面活性剂浓度对 BSA 一级和二级结构的影响。结果发现,在胶束前浓度下,BSA 的一级结构不受影响,但二级结构即 BSA 的α-螺旋结构发生了变化,如圆二色性所示。有趣的是,胶束后浓度的金属表面活性剂对 BSA 的一级和二级结构表现出明显的影响。SAXS 研究也支持了蛋白质展开及其围绕胶束包裹的事实。Zeta 电位描述了在不同浓度的金属表面活性剂存在下蛋白质的电荷和稳定性。同时,还发现蛋白质的存在延迟了金属表面活性剂的聚集行为,这是 BSA 与金属表面活性剂结合的标志。

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