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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Formation of a bovine serum albumin diligand complex with rutin and single-walled carbon nanotubes for the reduction of cytotoxicity
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Formation of a bovine serum albumin diligand complex with rutin and single-walled carbon nanotubes for the reduction of cytotoxicity

机译：用芦丁和单壁碳纳米管形成牛血清白蛋白杀络合物，用于减少细胞毒性

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Carbon nanotubes (CNTs) are extensively used in the area of biotechnology and biomedicine, and the binding of proteins to CNTs plays an important role in the potential toxicity of nanomaterials. Rutin is a glycoside of the bioactive quercetin with various health-improving effects due to its antioxidant ability. Demonstration of the interaction between serum albumin and bioactive components is important to design effective carriers for the suppression of CNTs' toxicity. In this study, bindings of bovine serum albumin (BSA) to single-walled CNTs and/or rutin were investigated by fluorescence and molecular docking techniques. The fluorescence of BSA was significantly quenched by both CNTs and rutin in static mode, which was confirmed by the Stern-Volmer calculations. Although rutin showed higher affinity to protein than CNTs, the interactions of both components with BSA did mainly locate within subdomain IIA (site I). BSA-diligand complexes were successfully formed after the simultaneous addition of CNTs and rutin. Bioactive rutin in the BSA-diligand complex still kept strong free radical scavenging activity compared to free rutin or BSA-monoligand complex. Consistently, the cytotoxicity of CNTs and reactive oxygen species formation in endothelial cells was reduced in the BSA-diligand complexes relative to those of BSA-CNTs corona or CNTs alone, where the co-presence of rutin played an important role. These findings suggest the possibility and advantage of designing BSA-based carriers for the suppression of CNTs' toxicity in their biomedical applications.
机译：碳纳米管（CNT）广泛用于生物医学和生物医学领域，蛋白质与CNT的结合在纳米材料的潜在毒性中起重要作用。芦丁是生物活性槲皮素的糖苷，由于其抗氧化能力，具有各种健康的效果。血清白蛋白和生物活性组分之间的相互作用的示范对于设计有效载体来抑制CNTS毒性是重要的。在该研究中，通过荧光和分子对接技术研究了牛血清白蛋白（BSA）与单壁CNT和/或芦丁的结合。 CNT和芦丁在静态模式下显着淬灭BSA的荧光，其通过船尾的转化计算证实。虽然芦丁表现出与CNT的蛋白质更高的亲和力，但两种组分与BSA的相互作用主要位于亚域IIa（Site i）内。在同时添加CNT和Rutin后成功形成BSA-稀释络合物。与免费的芦丁或BSA-单硅藻配合物相比，BSA-稀释和BSA-稀释度复合物中的生物活性芦丁仍然保持强烈的自由基清除活性。始终如一地，在BSA-ingigand络合物中相对于单独的BSA-CNTS Corona或CNTS的组综合体，在内皮细胞中形成CNT和反应性氧物种的细胞毒性，其中芦丁的共同存在发挥着重要作用。这些发现表明了设计基于BSA的载体的可能性和优点，用于抑制其生物医学应用中的CNTS毒性。

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