Spectroscopic studies on the interactions between CdTe quantum dots coated with different ligands and human serum albumin

Lai, Lu; Chen, Lin; Xu, Ziqiang; Han, Xiaojiao; Tian, Fang; Mei, Ping; Li, Dongwei; Ge, Yushu; Jiang, Feng-Lei; Zhang, Ye-Zhong; Liu, Yi

doi:10.1016/j.saa.2012.06.025

Cited by 76 publications

(46 citation statements)

References 42 publications

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“…The results show that the absorption intensities of HSA increased with increasing concentrations of complex I and decreased with the addition of complex II and also that the maximum absorption wavelength of HSA had a slight blue-shift which indicates that: (a) the interaction between two complexes and HSA induced the change in the α-helix structure of the protein and (b) the probable quenching mechanism of the fluorescence of HSA by Pd(II) complexes is static quenching, because dynamic quenching is largely caused by collision and the energy transfer from HSA to the quencher; meaning that the UV spectrum of HSA will not change. However, HSA-Pd(II) complexes which form from static quenching result in the changing UV spectrum of has, which is consistent with the fluorescence results [37,57,58].…”

Section: Uv-visible Spectral Studiessupporting

confidence: 88%

Biophysical study on the interaction between two palladium(II) complexes and human serum albumin by Multispectroscopic methods

Saeidifar

Mansouri‐Torshizi

Saboury

2015

Journal of Luminescence

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Section: Uv-visible Spectral Studiessupporting

confidence: 88%

Biophysical study on the interaction between two palladium(II) complexes and human serum albumin by Multispectroscopic methods

Saeidifar

Mansouri‐Torshizi

Saboury

2015

Journal of Luminescence

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“…14,39,40 Biological interactions between particles and proteins were more obvious for N-Cal than B-Cal based on fluorescence quenching assay results (Table 2); N-Cal had a three to four times higher quenching ratio. These results could be explained by the different specific surface areas of B-Cal and N-Cal and their different surface charges.…”

Section: Discussionmentioning

confidence: 99%

The fate of calcium carbonate nanoparticles administered by oral route: absorption and their interaction with biological matrices

Lee

Kim

et al. 2015

IJN

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Background Orally administered particles rapidly interact with biological fluids containing proteins, enzymes, electrolytes, and other biomolecules to eventually form particles covered by a corona, and this corona potentially affects particle uptake, fate, absorption, distribution, and elimination in vivo. This study explored relationships between the biological interactions of calcium carbonate particles and their biokinetics. Methods We examined the effects of food grade calcium carbonates of different particle size (nano [N-Cal] and bulk [B-Cal]: specific surface areas of 15.8 and 0.83 m 2 /g, respectively) on biological interactions in in vitro simulated physiological fluids, ex vivo biofluids, and in vivo in gastrointestinal fluid. Moreover, absorption and tissue distribution of calcium carbonates were evaluated following a single dose oral administration to rats. Results N-Cal interacted more with biomatrices than bulk materials in vitro and ex vivo, as evidenced by high fluorescence quenching ratios, but it did not interact more actively with biomatrices in vivo. Analysis of coronas revealed that immunoglobulin, apolipoprotein, thrombin, and fibrinogen, were the major corona proteins, regardless of particle size. A biokinetic study revealed that orally delivered N-Cal was more rapidly absorbed into the blood stream than B-Cal, but no significant differences were observed between the two in terms of absorption efficiencies or tissue distributions. Both calcium carbonates were primarily present as particulate forms in gastrointestinal fluids but enter the circulatory system in dissolved Ca 2+ , although both types showed partial phase transformation to dicalcium phosphate dihydrate. Relatively low dissolution (about 4%), no remarkable protein–particle interaction, and the major particulate fate of calcium carbonate in vivo gastrointestinal fluids can explain its low oral absorption (about 4%) regardless of particle size. Conclusion We conclude that calcium carbonate nanoparticles can act more actively with biological matrices in vitro and ex vivo, but that in vivo, their biological interactions and biokinetics are not affected by particle size.

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“…S20, a progressive decrease in the fluorescence intensity of fatal bovine serum was caused by quenching, accompanied by a red shift of maximum emission wavelength from 345.5 to 358.0 nm. According to the previous reports, the red shift can reasonably be attributed to an increased polarity of the region surrounding the tryptophan site (Lai et al, 2012). Proteins in FBS may be adsorbed onto negatively charged quantum dots to form a ''protein corona'' (Cedervall et al, 2007).…”

Section: The Interaction Of Cdte Qds With Serum Proteinsmentioning

confidence: 76%

“…A variety of molecular interactions can result in fluorescence quenching, including excited-state reactions, energy transfer, ground-state complex formation, and collisional quenching (Lai et al, 2012). Therefore, we investigated the interaction of QDs with fatal bovine serum using fluorescence spectroscopy.…”

Section: The Interaction Of Cdte Qds With Serum Proteinsmentioning

confidence: 99%

Necrotic cell death induced by the protein-mediated intercellular uptake of CdTe quantum dots

Lai

Jin

et al. 2015

Chemosphere

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Spectroscopic studies on the interactions between CdTe quantum dots coated with different ligands and human serum albumin

Cited by 76 publications

References 42 publications

Biophysical study on the interaction between two palladium(II) complexes and human serum albumin by Multispectroscopic methods

Biophysical study on the interaction between two palladium(II) complexes and human serum albumin by Multispectroscopic methods

The fate of calcium carbonate nanoparticles administered by oral route: absorption and their interaction with biological matrices

Necrotic cell death induced by the protein-mediated intercellular uptake of CdTe quantum dots

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