Human serum albumin stability and toxicity of anthraquinone dye alizarin complexone: An albumin–dye model

Ding, Fei; Zhang, Li; Diao, Jian-Xiong; Li, Xiu-Nan; Ma, Lin; Sun, Ying

doi:10.1016/j.ecoenv.2012.01.009

Cited by 30 publications

(8 citation statements)

References 59 publications

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“…In addition, the rhein-HSA complex showed major peaks at 228 nm and 434 nm and the absorbance of these peaks also increased as the concentrations of rhein increased. These observations indicate that rhein interacted with the tryptophan residue of HSA and changed the conformation of the HSA protein, which is in agreement with data obtained from the CD experiments and previously reported data (Ding et al, 2012). To further confirm this observation, the spectra of rhein (25 µM) with different concentrations of HSA (at 0.125, 0.25, and 0.5 mg/mL) were obtained (Figure 4b).…”

Section: Rhein Interacts With Hsa As Measured By Uv-vis Spectroscopysupporting

confidence: 90%

Bioactive anthraquinones found in plant foods interact with human serum albumin and inhibit the formation of advanced glycation endproducts

Liu¹,

Cai²,

Carley³

et al. 2018

Journal of Food Bioactives

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The glycation of human serum albumin (HSA) plays a critical role in the development of many disorders. Herein, the anti-glycation effects of several natural dietary anthraquinone derivatives including aloin, aloe-emodin, chrysophanol, emodin, physcion, and rhein were evaluated. The anthraquinones at 100 μM reduced fructose-, methylglyoxal-, and glyoxal-induced HSA glycation by 21% (aloe-emodin) to 92% (aloin), 17% (physcion) to 94% (emodin), and 16% (anthraquinone) to 67% (emodin), respectively. These anthraquinone derivatives also protected HSA by maintaining its free amino acid residues and secondary protein structure as characterized by circular dichroism. The mechanisms of their anti-glycation effects were investigated using rhein as a representative anthraquinone. The interactions between rhein and HSA were evaluated by biophysical characterizations, namely, isothermal titration calorimetry and UV-vis spectroscopy as well as computational modeling. Our findings suggest that the anti-glycation effects of these anthraquinones may be attributed to their binding capacity and stabilization of the HSA protein structure.

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Section: Rhein Interacts With Hsa As Measured By Uv-vis Spectroscopysupporting

confidence: 90%

Bioactive anthraquinones found in plant foods interact with human serum albumin and inhibit the formation of advanced glycation endproducts

Liu¹,

Cai²,

Carley³

et al. 2018

Journal of Food Bioactives

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“…The excitation wavelength was acquired by exciting the protein solution at 280 and 295 nm. 20 The emission spectra were gathered in the wavelength range of 290−500 and 300−500 nm corresponding to the excitation wavelength.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

Interactions of Fly Ash Particles with Mucin and Serum Albumin

et al. 2018

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Fly ash particles can contribute to haze and adverse health outcomes. In this study, two mucins, one from bovine submaxillary glands (bovine submaxillary mucin, BSM) and one from porcine stomach (porcine gastric mucin), as well as bovine serum albumin (BSA), which served as the physical barriers against foreign substances entering the tissues and the blood protein, respectively, were chosen as models for the investigations of the interactions between the proteins and the fly ash particles. Their adsorption behaviors were studied using spectroscopy and a quartz crystal microbalance with a dissipation monitor (QCM-D). The results indicated that the fly ash particles can induce the loosening of mucins and BSA, probably via the formation of complexes. Further, the secondary structure of proteins changed in the presence of fly ash particles. The α-helix content decreased with an increasing fly ash particle concentration. The addition of fly ash particles into protein solutions led to fluorescence quenching, which suggested that there were interactions between these particles and the mucins and BSA. The association constants ( K) for BSM and BSA were 5.35 and 4.18 L/g, respectively. Furthermore, the results of QCM-D analyses showed that the amount decreased on the mucin surface but increased slightly on the BSA surface, which indicated that the fly ash particles disrupted the mucin layer upon adsorption. These findings provide clear evidence of the interactions between the fly ash particles and the mucins and BSA, which can lead to structural changes. This study contributes to a better understanding of the interactions and adsorptions of atmospheric particulate pollutants with the proteins in the human body.

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“…Serum albumin, one of most abundant carrier proteins in plasma (7,8), plays an important role in the transport along with disposition of endogenous and exogenous ligands present in blood after binding. Research has been carried out on anthraquinones-binding properties with serum albumin using fluorescence techniques (14). This binding occurs reversibly due to the formation of non-covalent complexes influencing the characteristics of their physiological effects, thereby affecting the metabolism and excretion of various substances (10,11).…”

mentioning

confidence: 99%

“…The results of these various binding studies may be useful in designing new and promising drugs for a variety of medical conditions in clinic. Research has been carried out on anthraquinones-binding properties with serum albumin using fluorescence techniques (14). In view of importance of this class of molecule, as a potential candidate for drug action, the focus of this study was to elucidate the nature of interactions of parent molecule with HSA.…”

mentioning

confidence: 99%

Investigation for the Interaction of Tyramine‐Based Anthraquinone Analogue with Human Serum Albumin by Optical Spectroscopic Technique

et al. 2012

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A newly synthesized anthraquinone derivative 'N-(2-methylanthraquinone)-4-(2-aminoethyl) phenol' (Tyan) were characterized as a fluorophore from photophysical analysis by measuring the UV-Vis absorptive (λ(ex) = 325 nm) and fluorescence emitive (λ(em) = 660 nm) values. Density functional theory additionally supported the spectroscopic data by modulation of highest occupied molecular orbital rather than lowest unoccupied molecular orbital due to the affect of tyramine moiety present in Tyan. The pharmacological importance of Tyan was evaluated by molecular docking with human serum albumin. The molecular docking of the Tyan was performed with the crystal structure of human serum albumin (PDB entry 1E78), which shows binding in all the three domains of human serum albumin corresponding to -7.74 as the GScore. Moreover, the interactions of human serum albumin with Tyan were assessed employing fluorescence spectroscopy under simulative physiological conditions, and the binding constant for the interaction at 25 °C was found to be 0.6 × 10(3)/M.

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Human serum albumin stability and toxicity of anthraquinone dye alizarin complexone: An albumin–dye model

Cited by 30 publications

References 59 publications

Bioactive anthraquinones found in plant foods interact with human serum albumin and inhibit the formation of advanced glycation endproducts

Bioactive anthraquinones found in plant foods interact with human serum albumin and inhibit the formation of advanced glycation endproducts

Interactions of Fly Ash Particles with Mucin and Serum Albumin

Investigation for the Interaction of Tyramine‐Based Anthraquinone Analogue with Human Serum Albumin by Optical Spectroscopic Technique

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