β-Carotene and astaxanthin with human and bovine serum albumins

Li, Xiangrong; Wang, Gongke; Chen, Dejun; Lü, Yan

doi:10.1016/j.foodchem.2015.01.133

Cited by 98 publications

(47 citation statements)

References 34 publications

(39 reference statements)

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“…Negative values of Δ H and positive values of Δ S at all studied temperature levels suggest that the binding of MLN8237 with HSA is predominantly driven by entropy. However, the same results were reported for several other protein–ligand complexes by using ITC or fluorescence spectroscopic methods3132. The process is ubiquitous throughout protein–ligand interactions.…”

Section: Resultssupporting

confidence: 75%

Domain-specific interactions between MLN8237 and human serum albumin estimated by STD and WaterLOGSY NMR, ITC, spectroscopic, and docking techniques

Yang

Liu

Huang

et al. 2017

Sci Rep

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Alisertib (MLN8237) is an orally administered inhibitor of Aurora A kinase. This small-molecule inhibitor is under clinical or pre-clinical phase for the treatment of advanced malignancies. The present study provides a detailed characterization of the interaction of MLN8237 with a drug transport protein called human serum albumin (HSA). STD and WaterLOGSY nuclear magnetic resonance (NMR)-binding studies were conducted first to confirm the binding of MLN8237 to HSA. In the ligand orientation assay, the binding sites of MLN8237 were validated through two site-specific spy molecules (warfarin sodium and ibuprofen, which are two known site-selective probes) by using STD and WaterLOGSY NMR competition techniques. These competition experiments demonstrate that both spy molecules do not compete with MLN8237 for the specific binding site. The AutoDock-based blind docking study recognizes the hydrophobic subdomain IB of the protein as the probable binding site for MLN8237. Thermodynamic investigations by isothermal titration calorimetry (ITC) reveal that the non-covalent interaction between MLN8237 and HSA (binding constant was approximately 105 M−1) is driven mainly by favorable entropy and unfavorable enthalpy. In addition, synchronous fluorescence, circular dichroism (CD), and 3D fluorescence spectroscopy suggest that MLN8237 may induce conformational changes in HSA.

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Section: Resultssupporting

confidence: 75%

Domain-specific interactions between MLN8237 and human serum albumin estimated by STD and WaterLOGSY NMR, ITC, spectroscopic, and docking techniques

Yang

Liu

Huang

et al. 2017

Sci Rep

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“…The non‐linear nature of the Stern–Volmer plot indicates the involvement of other factors apart from static quenching, such as dynamic quenching . To explain the nonlinearity of the curve, these systems were treated in terms of the ‘sphere‐of‐action’ model, the equation that describes this situation is :

F_{0} true/ F = normalexp ((), K_{a} ([], Q))

where K a is the binding constant. In the present case, the experimental results exhibit a very good linear relationship between ln ( F 0 / F ) and [ Q ] (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The non-linear nature of the Stern-Volmer plot indicates the involvement of other factors apart from static quenching, such as dynamic quenching (35). To explain the nonlinearity of the curve, these systems were treated in terms of the 'sphere-of-action' model, the equation that describes this situation is (6,36):…”

Section: Resultsmentioning

confidence: 99%

Study on the interaction of β‐carotene and astaxanthin with trypsin and pepsin by spectroscopic techniques

Peihong

2015

Luminescence

Self Cite

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β-Carotene and astaxanthin are two carotenoids with powerful antioxidant properties, but the binding mechanisms of β-carotene/astaxanthin to proteases remain unclear. In this study, the interaction of these two carotenoids with trypsin and pepsin was investigated using steady-state and time-resolved fluorescence measurements, synchronous fluorescence spectroscopy, UV-vis absorption spectroscopy and circular dichroism (CD) spectroscopy. The experimental results indicated that the quenching mechanisms of trypsin/pepsin by the two carotenoids are static processes. The binding constants of trypsin and pepsin with these two carotenoids are in the following order: astaxanthin-trypsin > astaxanthin-pepsin > β-carotene-trypsin > β-carotene-pepsin, respectively. Thermodynamic investigations revealed that the interaction between the two carotenoids and trypsin/pepsin is synergistically driven by enthalpy and entropy, and hydrophobic forces and electrostatic attraction have a significant role in the reactions. In addition, as shown by synchronous fluorescence spectroscopy, UV-vis absorption spectroscopy and CD, the two carotenoids may induce conformational and microenvironmental changes in trypsin/pepsin. The study provides an accurate and full basic data for clarifying the binding mechanisms of the two carotenoids with trypsin/pepsin and is helpful in understanding their effect on protein function and their biological activity in vivo.

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“…have shown that the cochineal red A resulted in conformational alteration of serum albumins based on UV–vis, fluorescence, and Fourier transform infrared (FTIR) spectroscopy . Lu investigated the effects of β‐carotene and astaxanthin with human and bovine serum albumins based on fluorescence measurements, UV–vis spectrophotometry, and FTIR measurements . For CA as a widely used food additive and colorant, it is important to study how it influences the structure and physiological function of human proteins such as HSA.…”

Section: Introductionmentioning

confidence: 99%

Exploration of interaction of canthaxanthin with human serum albumin by spectroscopic and molecular simulation methods

et al. 2017

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The interaction between the food colorant canthaxanthin (CA) and human serum albumin (HSA) in aqueous solution was explored by using fluorescence spectroscopy, three-dimensional fluorescence spectra, synchronous fluorescence spectra, UV-vis absorbance spectroscopy, circular dichroism (CD) spectra and molecular docking methods. The thermodynamic parameters calculated from fluorescence spectra data showed that CA could result in the HSA fluorescence quenching. From the K change with the temperature dependence, it was concluded that HSA fluorescence quenching triggered by CA is the static quenching and the number of binding sites is one. Furthermore, the secondary structure of HSA was changed with the addition of CA based on the results of synchronous fluorescence, three-dimensional fluorescence and CD spectra. Hydrogen bonds and van der Waals forces played key roles in the binding process of CA with HSA, which can be obtained from negative standard enthalpy (ΔH) and negative standard entropy (ΔS). Furthermore, the conclusions were certified by molecular docking studies and the binding mode was further analyzed with Discovery Studio. These conclusions can highlight the potential of the interaction mechanism of food additives and HSA.

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β-Carotene and astaxanthin with human and bovine serum albumins

Cited by 98 publications

References 34 publications

Domain-specific interactions between MLN8237 and human serum albumin estimated by STD and WaterLOGSY NMR, ITC, spectroscopic, and docking techniques

Domain-specific interactions between MLN8237 and human serum albumin estimated by STD and WaterLOGSY NMR, ITC, spectroscopic, and docking techniques

Study on the interaction of β‐carotene and astaxanthin with trypsin and pepsin by spectroscopic techniques

Exploration of interaction of canthaxanthin with human serum albumin by spectroscopic and molecular simulation methods

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