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

Luo, Mengjuan; Sui, Yinhua; Tian, Rong; Lu, Naihao

doi:10.1016/j.bpc.2020.106327

Cited by 11 publications

(10 citation statements)

References 32 publications

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“…The cytotoxicity of heme and oxidative stress in endothelial cells were decreased in the BSA-diligand complexes relative to those of heme or BSA-heme complexes, and 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 biomedical applications [56]. Apart from this, rutin has also been applied in industry as a colorant, stabilizer, and preservative for food [57].…”

Section: Discussionmentioning

confidence: 91%

In Vitro and In Silico Interaction Studies with Red Wine Polyphenols against Different Proteins from Human Serum

Shafreen¹,

Lakshmi

Pandian

et al. 2021

Molecules

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Previous reports have shown that consumption of wine has several health benefits; however, there are different types of wine. In the present study, red wines were investigated for their compositions of active ingredients. The interaction of each component in terms of its binding mode with different serum proteins was unraveled, and the components were implicated as drug candidates in clinical settings. Overall, the study indicates that red wines have a composition of flavonoids, non-flavonoids, and phenolic acids that can interact with the key regions of proteins to enhance their biological activity. Among them, rutin, resveratrol, and tannic acid have shown good binding affinity and possess beneficial properties that can enhance their role in clinical applications.

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Section: Discussionmentioning

confidence: 91%

In Vitro and In Silico Interaction Studies with Red Wine Polyphenols against Different Proteins from Human Serum

Shafreen¹,

Lakshmi

Pandian

et al. 2021

Molecules

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“…It is of great interest to develop effective carriers that can simultaneously encapsulate and protect several bioactive components. ,,,, Our previous study has demonstrated the generation of the BSA–diligand complex with carbon nanotubes and quercetin for the protection of bioactive components and inhibition of nanotubes’ cytotoxicity . Although the generation of the BSA–monoligand complex is widely reported, ,− the formation of a BSA–multiligand complex with bioactive flavonoids and free Cu(II) is still scarcely investigated.…”

Section: Introductionmentioning

confidence: 99%

Bovine Serum Albumin as a Potential Carrier for the Protection of Bioactive Quercetin and Inhibition of Cu(II) Toxicity

Lan

Pi³

et al. 2022

Chem. Res. Toxicol.

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Considering the protective ability of proteins and the potential toxicity of free Cu(II), it was proposed herein that the co-presence of protein could play an important role in suppressing the toxicity of free Cu(II) to the stability of bioactive quercetin if a flavonoid–protein–Cu(II) complex could be formed. In this study, the interaction between quercetin (a major flavonoid in the human diet) and bovine serum albumin (BSA) was investigated in the absence and presence of free Cu(II). The results demonstrated that both quercetin and free Cu(II) had a strong ability to quench the intrinsic fluorescence of BSA through a static procedure (i.e., formation of a BSA–monoligand complex). Site marker competitive experiments illustrated that the binding of both quercetin and Cu(II) to BSA mainly took place in subdomain IIA. The quenching process of free Cu(II) with BSA was easily affected by quercetin, and the increased binding capacity possibly resulted from the generation of a ternary quercetin–BSA–Cu(II) complex. The stability and free radical scavenging activity of bioactive quercetin during incubation was promoted in the BSA–diligand complex relative to a quercetin–Cu(II) complex. A quercetin–Cu(II) system could generate reactive oxygen species such as hydrogen peroxide (H2O2) and hydroxyl radicals (•OH), which were significantly inhibited upon BSA binding. Consistently, the cytotoxicity of the quercetin–Cu(II) system to endothelial cells was decreased in the BSA–diligand complex, where the co-presence of BSA played an important role. These results suggest the possibility and advantage of developing albumin-based carriers for the protection of bioactive components and suppression of Cu(II) toxicity in their biomedical and nutritional applications.

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“…These findings demonstrated that the serum albumin–diligand complex provided a better inhibition on the cytotoxicity of heme than did serum albumin–monoligand complex, in which the simultaneous presence of quercetin in the complex played an important role in free radical scavenging and suppression of oxidative stress. Recently, we have demonstrated that the formation of BSA–diligand complex with rutin and heme provides a better inhibition on the cytotoxicity of heme than did protein–monoligand complex . Bioactive rutin in the BSA–diligand complex still kept strong antioxidant activity compared to free rutin, whereas the stability and antioxidant activity of bioactive quercetin was promoted in the BSA–diligand complex relative to free flavonoid (Figure ).…”

Section: Results and Discussionmentioning

confidence: 97%

“…Free heme exhibits high cytotoxic effects on different cells and causes tissue damage. It has been shown that serum albumin could reduce the toxic effects of free heme by generating serum albumin–heme complex. − , To mimic H 2 O 2 production in vivo, glucose oxidase (GO)/glucose system was used to generate H 2 O 2 . First, we examined the cytotoxicity of heme, GO or quercetin to endothelial cells.…”

Section: Results and Discussionmentioning

confidence: 99%

“…Recently, we have demonstrated that the formation of BSA−diligand complex with rutin and heme provides a better inhibition on the cytotoxicity of heme than did protein−monoligand complex. 34 Bioactive rutin in the BSA−diligand complex still kept strong antioxidant activity compared to free rutin, 34 whereas the stability and antioxidant activity of bioactive quercetin was promoted in the BSA− diligand complex relative to free flavonoid (Figure 5). The formation of BSA−diligand complex in this study will provide an additional protection against instability of bioactive quercetin.…”

Section: Resultsmentioning

confidence: 99%

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Generation of a Bovine Serum Albumin–Diligand Complex for the Protection of Bioactive Quercetin and Suppression of Heme Toxicity

Lan

Luo

Tian

et al. 2021

Chem. Res. Toxicol.

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As an abundant protein in milk and blood serum, bovine serum albumin (BSA) contains various sites to bind a lot of bioactive components, generating BSA− monoligand complex. Demonstration of the interaction between BSA and bioactive components (such as heme, flavonoids) is important to develop effective carrier for the protection of bioactive ligands and to reduce cytotoxicity of heme. Herein, the bindings of BSA to quercetin and/or heme were investigated by multispectroscopic and molecular docking methods. The fluorescence of protein was significantly quenched by both quercetin and heme in a static mode (i.e., generation of BSA−ligand complex). Although quercetin had lower affinity to protein than heme, the interactions of both compounds with protein did locate in site I (i.e., subdomain IIA). BSA−diligand complex was successfully generated after the coaddition of quercetin and heme. The cytotoxicity of free heme to endothelial cells was reduced in the BSA−diligand complex relative to that of heme or BSA− monoligand complex, while the stability of bioactive quercetin was promoted in the complex relative to free flavonoid. The complex provided a better inhibition on the cytotoxicity of heme than BSA−monoligand complex, in which the copresence of quercetin played a vital role.

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

Cited by 11 publications

References 32 publications

In Vitro and In Silico Interaction Studies with Red Wine Polyphenols against Different Proteins from Human Serum

In Vitro and In Silico Interaction Studies with Red Wine Polyphenols against Different Proteins from Human Serum

Bovine Serum Albumin as a Potential Carrier for the Protection of Bioactive Quercetin and Inhibition of Cu(II) Toxicity

Generation of a Bovine Serum Albumin–Diligand Complex for the Protection of Bioactive Quercetin and Suppression of Heme Toxicity

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