Interaction of isofraxidin with human serum albumin

Liu, Jiaqin; Tian, Jianniao; Tian, Xuan; Hu, Zhide; Chen, Xingguo

doi:10.1016/j.bmc.2003.10.030

Cited by 125 publications

(55 citation statements)

References 23 publications

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“…Many studies on small molecules, such as drugs and dyes binding to protein (BSA, HSA, etc.) (1,(7)(8)(9)(10) and DNA (11) have been reported. Serum albumin is the most abundant protein in the circulatory system, accounting for 60% of the total serum protein (12)(13)(14).…”

Section: Introductionmentioning

confidence: 97%

Studies on the interaction between tetraphenylporphyrin compounds and bovine serum albumin

et al. 2007

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The interaction of three porphyrin compounds with bovine serum albumin (BSA) was examined by fluorescence emission spectra at the excitation wavelength 280 nm and in UV-Vis absorption spectra. Through fluorescence quenching experiments, it was confirmed that the combination of three porphyrin compounds with BSA was a single static quenching process. The binding constant K(A), the thermodynamic parameters enthalpy change (DeltaH(0)), Gibbs free energy change (DeltaG(0)) and entropy change (DeltaS(0)) were obtained. It was found that hydrophobic interaction played a main role in tetraphenylporphyrin (TPP) or tetraparacholophenylporphyrin (TClPP) binding to BSA, while tetraparamethoxyphenylporphyrin (TMEOPP) mainly based on van der Waals' force. According to Föster energy transfer, the separate distance r, the energy transfer efficiency E and Föster radium R(0) were calculated. The results obtained from the above experiments showed that three porphyrin compounds were tightly bound to BSA.

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Section: Introductionmentioning

confidence: 97%

Studies on the interaction between tetraphenylporphyrin compounds and bovine serum albumin

et al. 2007

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“…Figure 1 shows the CD spectra in which two negative bands are visible in the far-UV region at 208 nm and 222 nm. These are characteristic of the α-helical structures of protein (Liu et al, 2004). Figure 1a shows that the CD spectrum of BSA standard solution almost overlapped with those of uncoated and 0.25% alginate-coated liposomes, suggesting that the secondary structure of BSA was preserved throughout the coating, drying and rehydration processes.…”

Section: Characterization Of Spray-dried Liposomesmentioning

confidence: 79%

The effect of polymer coatings on physicochemical properties of spray-dried liposomes for nasal delivery of BSA

Chen

Sabatino

Albertini

et al. 2013

European Journal of Pharmaceutical Sciences

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“…Studies on the interactions between surfactants and proteins would be beneficial for understanding the occurence of surfactants acting as solubilizing or denaturing agents for proteins [7,8]. For example, serum albumins are the most abundant proteins in blood plasma and are the major soluble protein in the circulatory system [9].…”

Section: Introductionmentioning

confidence: 99%

Fluorescence Spectroscopy Study on the Interaction of Acetal Cleavable Anionic Surfactants and Bovine Serum Albumin

et al. 2014

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The interactions between bovine serum albumin (BSA) and two cleavable anionic surfactants, sodium 3-[(2-nonyl-1,3-dioxolan-4-yl)methoxy]propane-1-sulfonate (SNPS) and sodium 3,3 -(2-nonyl-1,3-dioxane-5,5-diyl)bis(methylene)bis(oxy)dipropane-1-sulfonate (SNDPS), have been studied by means of fluorescence spectroscopy and thermodynamic analysis. The fluorescence of BSA is quenched via a static quenching mechanism with the addition of the surfactants. The binding constants of the surfactants and proteins have been measured, with (SNPS) = 8.71 × 10 4 M −1 and (SNDPS) = 7.08 × 10 4 M −1 , respectively. The interaction between surfactants and BSA is mainly of hydrophobic nature, based on the number of binding sites, n[n(SNPS) = 1.57, n(SNDPS) = 1.47], and the thermodynamic relationship. These results suggest that SNPS and SNDPS could be effective protein denaturants for protein separation and analysis.

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Interaction of isofraxidin with human serum albumin

Cited by 125 publications

References 23 publications

Studies on the interaction between tetraphenylporphyrin compounds and bovine serum albumin

Studies on the interaction between tetraphenylporphyrin compounds and bovine serum albumin

The effect of polymer coatings on physicochemical properties of spray-dried liposomes for nasal delivery of BSA

Fluorescence Spectroscopy Study on the Interaction of Acetal Cleavable Anionic Surfactants and Bovine Serum Albumin

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