Studies of the interaction between apigenin and bovine serum albumin by spectroscopic methods

Shang, Yonghui; Li, Hua

doi:10.1134/s1070363210080232

Cited by 8 publications

(4 citation statements)

References 33 publications

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“…Our results for K sv , K a , n and the thermodynamic parameters (negative values of DH and DS, see below) agree with previous data reported for apigenin [71]. On the other hand, it is important to mention that there are some discrepancies in the literature for the interaction of apigenin with bovine serum albumin being the K sv , K a or the thermodynamic parameters quite different from each other [72][73][74]. These differences have been attributed to the different experimental conditions used in each determination [74] (differences in albumin and flavonoid concentrations, albumin fractions and/or dissolution media: pH values and the concentrations of NaCl and Mg 2+ ).…”

Section: Binding Constants and The Number Of Binding Sitessupporting

confidence: 91%

Apigenin oxidovanadium(IV) cation interactions. Synthesis, spectral, bovine serum albumin binding, antioxidant and anticancer studies

Medina

Naso

Pérez

et al. 2017

Journal of Photochemistry and Photobiology A: Chemistry

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Continuing and expanding our previous work on flavonoid oxidovanadium(IV) (VO) metal complexes as possible anti-cancer agents, the VOapigenin compound was synthesized and characterized. An "acetylacetone-like" coordination through the C¼O and OÀ À moieties of the ligand to the metal center with one apigenin ligand per metal ion was assumed using different spectroscopies and elemental analysis as well as thermal measurements. The vibrational experimental spectrum of VOapigenin was supported by theoretical calculations. According to the structure of the flavonoid it exerted mild antioxidant properties that were enhanced by metal coordination. The compounds showed moderate anticancer activity on lung A549 and cervix HeLa cancer cell lines, displaying an incubation time dependent behavior. Cellular increase of reactive oxygen species (ROS) and glutathione depletion have been measured upon incubation with the compounds. These cell killing activities were reverted when natural antioxidants were incubated with the compounds and the addition of the antioxidant agent Nacetylcysteine generated depletion of the cellular ROS levels. Therefore, a stress oxidative mechanism of action has been assumed. Moreover, the compounds showed no toxicity against Artemia salina and were not mutagenic. Both apigenin and the complex could be transported and stored by bovine serum albumin with similar binding constants and mechanisms than other VOflavonoid complexes.

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Section: Binding Constants and The Number Of Binding Sitessupporting

confidence: 91%

Apigenin oxidovanadium(IV) cation interactions. Synthesis, spectral, bovine serum albumin binding, antioxidant and anticancer studies

Medina

Naso

Pérez

et al. 2017

Journal of Photochemistry and Photobiology A: Chemistry

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“…The distance between apigenin and HSA is close enough (3.21 nm) to favor non-radiation energy transfer from HSA to apigenin. Apigenin interaction with BSA (Shang & Li, 2010) is similar to HSA with binding constants, and number of binding sites is summarized in Table 4. The thermodynamic parameters ( Table 7) are indicative of hydrogen bonding and hydrophobic interactions in apigenin-BSA interaction.…”

Section: Flavone-sa Interactionmentioning

confidence: 99%

A review on structure–affinity relationship of dietary flavonoids with serum albumins

Pal

Saha

2013

Journal of Biomolecular Structure and Dynamics

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Flavonoids are a class of plant secondary metabolites and among thousands of flavonoids few are considered as dietary flavonoids. Serum albumin (SA), the most abundant protein in plasma, functions as the most important carrier of vital drugs, including dietary flavonoids. The binding affinity of dietary flavonoids to SA is demonstrated to be governed by structure-affinity relationship (SAR) and its bioavailability. The present review summarizes the interactions of flavonoids categorized as flavanol, flavonol, flavone, isoflavone, flavanones, and anthocyanidins with SAs (bovine serum albumin and human serum albumin) in light of SAR. The key findings are: (1) the position and degree of hydroxylation highly influence the affinity of flavonoids to SAs, (2) glycosylation decreases and substitution of methoxy group increases the affinity of flavonoids for SAs, (3) catechin gallates have higher binding affinity to SAs than catechins and gallocatechins, (4) inorganic metal ions modulate the binding affinity of flavonoids to SAs, and (5) hydrophobic interaction plays a major role in the interactions of all flavonoids with SAs.

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“…Molecular docking can intuitively show the process and results of the interaction between molecules and proteins [22][23][24]. Shang et al determined the binding constant (K A ) and binding site number (n) of hesperidin and glycoside hesperidin with bovine serum albumin (BSA) by fluorescence spectrometry [25]. Tan et al simulated the interaction between PBDEs and human serum albumin (HSA) by molecular docking [26].…”

Section: Introductionmentioning

confidence: 99%

A Pilot Study on the Concentration, Distribution and Bioaccumulation of Polybrominated Diphenyl Ethers (PBDEs) in Tissues and Organs of Grassland Sheep

Chen

Yang

Bao

et al. 2022

IJERPH

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Polybrominated diphenyl ether (PBDE) concentrations in various tissues and organs of grassland sheep from Inner Mongolia, China, were determined. The abilities of PBDEs binding to ovine serum albumin (OSA) and Cytochrome P450 enzyme (CYP3A24) were assessed by fluorescence spectroscopy and molecular docking simulations. The PBDE concentrations in the sheep tissue and organ samples were 33.4–167 pg/g dw. The distribution of PBDEs in sheep organs and tissues is affected not only by the function of organs and tissues, but also by the characteristics of PBDEs. Adipose tissue tends to bioaccumulate more-brominated BDEs (BDE-154, -153, and -183), but muscle tissues and visceral organs mainly bioaccumulate less-brominated BDEs. The distribution of PBDEs in visceral organs is mainly affected by the transport of ovine serum albumin (OSA) and the metabolism of CYP3A24 enzyme. The distribution of PBDEs in adipose tissue and brain is mainly affected by their logKOW.

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Studies of the interaction between apigenin and bovine serum albumin by spectroscopic methods

Cited by 8 publications

References 33 publications

Apigenin oxidovanadium(IV) cation interactions. Synthesis, spectral, bovine serum albumin binding, antioxidant and anticancer studies

Apigenin oxidovanadium(IV) cation interactions. Synthesis, spectral, bovine serum albumin binding, antioxidant and anticancer studies

A review on structure–affinity relationship of dietary flavonoids with serum albumins

A Pilot Study on the Concentration, Distribution and Bioaccumulation of Polybrominated Diphenyl Ethers (PBDEs) in Tissues and Organs of Grassland Sheep

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