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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 for the suppression of heme toxicity
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Formation of a bovine serum albumin diligand complex with rutin for the suppression of heme toxicity

机译：用芦丁形成牛血清白蛋白杀络合物，用于抑制血红素毒性

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Serum albumin binds avidly to heme to form heme-serum albumin complex and can protect against the potentially toxic effects of heme. Rutin is a glycoside of the bioflavonoid quercetin with various protective effects due to its antioxidant ability. Clarification of the interaction mechanisms between serum albumin and bioactive components (such as heme and flavonoid) is important to develop effective carriers for encapsulation of heme and suppression of its toxicity. In this study, bindings of bovine serum albumin (BSA) to heme and/or rutin were investigated by experimental and molecular docking techniques. The fluorescence of BSA was quenched by both heme and rutin in static mode (i.e. formation of BSA-monoligand complexes), which was confirmed by Stern-Volmer calculations. Although heme showed higher affinity to BSA than rutin, the interactions of both components with BSA did locate within subdomain EA (site I). BSA-diligand complexes were successfully formed after the simultaneous addition of heme and rutin. Bioactive rutin in the BSA-diligand complex still kept strong free radical scavenging activity compared to free rutin or BSA-monoligand complex. Hydrogen peroxide (H2O2)-induced heme degradation and free iron release was inhibited upon BSA binding and further decreased in BSA-diligand complexes. Consistently, the cytotoxicity of heme and oxidative stress in endothelial cells was decreased in the BSA-diligand complexes relative to those of heme or BSA-heme complex, where the co-presence of rutin played an important role. These results suggest the possibility and advantage of developing BSA-based carriers for the suppression of heme toxicity in their biomedical applications.
机译：血清白蛋白杀菌地与血红素结合，形成血红素血清白蛋白复合物，可以防止血红素的潜在毒性作用。芦丁是生物鳞状蛋白槲皮素的糖苷，由于其抗氧化能力，具有各种保护作用。澄清血清白蛋白和生物活性成分（如血红素和黄酮）之间的相互作用机制对于开发有效载体来封装血红素和抑制其毒性。在该研究中，通过实验和分子对接技术研究了牛血清白蛋白（BSA）与血红素和/或芦丁的结合。在静态模式中，通过血红素和芦丁淬灭BSA的荧光（即BSA-单机凝聚配合物的形成），通过船尾的转化计算证实。虽然血红素对BSA具有比芦丁更高的亲和力，但两种组分与BSA的相互作用所做的确实位于亚域EA（Site i）内。在同时添加血红素和芦丁后成功形成了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。在BSA结合时抑制过氧化氢（H 2 O 2）诱导的血红液降解和游离铁释放，并在BSA-稀释配合物中进一步降低。始终如一地，在与血红素或Bsa-Heme络合物的BSA-稀释络合物中，内皮细胞中血红素细胞细胞毒性和氧化应激的细胞毒性降低，其中芦丁的共同存在起着重要作用。这些结果表明了在其生物医学应用中抑制血红素毒性的基于BSA的载体的可能性和优点。

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