Insights into the effect of N-acetyl-L-cysteine-capped CdTe quantum dots on the structure and activity of human serum albumin by spectroscopic techniques

Sun, Haoyu; Yang, Xudan; Li, Meng; Han, Songlin; Liu, Yingxue; Tan, Xue-Jie; Liu, Rutao

doi:10.1016/j.jlumin.2015.06.005

Cited by 13 publications

(5 citation statements)

References 48 publications

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“…To account for the existence of the inner filter effect, the fluorescence intensity values of the samples need to be corrected for their absorption at excitation and emission wavelengths using the relationship equation

F_{c o r} italic= F_{o b s} italic\times 1 0^{((), A_{ex} italic+ A_{e m}) true/ italic2}

where F cor and F obs are the corrected and observed fluorescence intensities, respectively, and A ex and A em are the absorbance values of the system at the excitation and emission wavelengths, respectively. The fluorescence intensity used in this article was corrected.…”

Section: Methodsmentioning

confidence: 99%

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Spectroscopy and molecular docking study on the interaction of daidzein and genistein with pepsin

Nan

Wang²,

Sun

et al. 2016

Luminescence

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The interaction of pepsin with daidzein (Dai) or genistein (Gen) was investigated using spectroscopic techniques under simulated physiological conditions. Dai and Gen can quench the fluorescence of pepsin and the quenching mechanism was a static process. The binding site number n and apparent binding constant K were measured at different temperatures. The thermodynamic parameters ΔΗ, ΔG and ΔS were calculated. The results indicated that van der Waals forces and hydrogen bond formation played major roles in the interaction of Dai or Gen with pepsin. The binding distance between pepsin and Dai or Gen was calculated according to energy transfer theory. The results of synchronous fluorescence spectra showed that the microenvironment and conformation of pepsin were changed. UV absorption and 3D fluorescence spectra showed that the binding interaction disturbed the microenvironment of amino acid residues and induced conformational changes in pepsin. Molecular docking results showed that Dai and Gen entered into the hydrophobic cavity of pepsin and two hydrogen bonds formed between Dai or Gen and pepsin. The results demonstrated that the interaction behavior between Dai and Gen with pepsin was slightly different, which denoted that the 5-hydroxyl group of Gen, to a certain extent, had an effect on ligand binding to proteins. Copyright © 2016 John Wiley & Sons, Ltd.

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F_{c o r} italic= F_{o b s} italic\times 1 0^{((), A_{ex} italic+ A_{e m}) true/ italic2}

Section: Methodsmentioning

confidence: 99%

Section: Fluorescence Quenching and Synchronous Fluorescencementioning

confidence: 99%

Spectroscopy and molecular docking study on the interaction of daidzein and genistein with pepsin

Nan

Wang²,

Sun

et al. 2016

Luminescence

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show abstract

“…Moreover, the quenching information was further verified by the amendatory Stern-Volmer equation (Liang et al, 2008;Asha Jhonsi et al, 2009;Sun et al, 2015).…”

Section: Effects Of Reaction Timementioning

confidence: 96%

Study on AgInZnS-Graphene Oxide Non-toxic Quantum Dots for Biomedical Sensing

et al. 2020

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In recent years, non-toxic quantum dot has caught the attention of biomedical fields. However, the inherent cytotoxicity of QDs makes its biomedical application painful, and is a major drawback of this method. In this paper, a non-toxic and water-soluble quantum dot AgInZnS-GO using graphene oxide was synthesized. A simple model of state complex was also established, which is produced through a combination of quantum dots and protein. The interaction between AIZS-GO QDs and human serum albumin (HSA) has significant meaning in vivo biological application. Herein, the binding of AIZS-GO QDs and HSA were researched using fluorescence spectra, Uv-visible absorption spectra, FT-IR spectra, and circular dichroism (CD) spectra. The results of fluorescence spectra demonstrate that AIZS-GO QDs have an obvious fluorescence quenching effect on HSA. The quenching mechanism is static quenching, which implies that some type of complex was produced by the binding of QDs and HSA. These results were further proved by Uv-visible absorption spectroscopy. The Stern-Volmer quenching constant K sv at various temperatures (298 K, 303 K, 308 K) were acquired from analyzing Stern-Volmer plots of the fluorescence quenching information. The Van't Hoff equation could describe the thermodynamic parameters, which demonstrated that the van der Waals and hydrogen bonds had an essential effect on the interaction. FT-IR spectra and CD spectra further indicate that AIZS-GO QDs can alter the structure of HSA. These spectral methods show that the quantum dot can combine well with HSA. The experimental results showed that AgInZn-GO water-soluble quantum dots have good biocompatibility, which can be combined with proteins to form new compounds which have no cytotoxicity and biological practicability. It provides an important basis for the combination of quantum dots and specific proteins as well as fluorescent labeling.

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“…The role of the protein corona masking the designed surface chemistry of QDs is a critical issue because cellular uptake, and its associated physiological response, are regulated by chemical interactions at the nanoparticle surface. The interactions between QDs and serum proteins may impose severe impacts on the function of the proteins and hence cause toxicity [ 14 , 15 , 16 ]. Therefore, it is important to examine the interactions between QDs and proteins, which can help understanding the mechanisms of the biological effects of QDs.…”

Section: Introductionmentioning

confidence: 99%

Probing Temperature- and pH-Dependent Binding between Quantum Dots and Bovine Serum Albumin by Fluorescence Correlation Spectroscopy

et al. 2017

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Luminescent quantum dots (QDs) with unique optical properties have potential applications in bio-imaging. The interaction between QDs and bio-molecules is important to the biological effect of QDs in vivo. In this paper, we have employed fluorescence correlation spectroscopy (FCS) to probe the temperature- and pH-dependent interactions between CdSe QDs with carboxyl (QDs-COOH) and bovine serum albumin (BSA) in buffer solutions. The results have shown that microscopic dissociation constant K′D is in the range of (1.5 ± 0.2) × 10−5 to (8.6 ± 0.1) × 10−7 M, the Hill coefficient n is from 0.4 to 2.3, and the protein corona thickness is from 3.0 to 9.4 nm. Variable-temperature measurements have shown both negative values of ∆H and ∆S for BSA adsorption on QDs-COOH, while pH has a profound effect on the adsorption. Additional, FCS measurement QDs-COOH and proteins in whole mice serum and plasma samples has also been conducted. Finally, simulation results have shown four favored QD binding sites in BSA.

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Insights into the effect of N-acetyl-L-cysteine-capped CdTe quantum dots on the structure and activity of human serum albumin by spectroscopic techniques

Cited by 13 publications

References 48 publications

Spectroscopy and molecular docking study on the interaction of daidzein and genistein with pepsin

Spectroscopy and molecular docking study on the interaction of daidzein and genistein with pepsin

Study on AgInZnS-Graphene Oxide Non-toxic Quantum Dots for Biomedical Sensing

Probing Temperature- and pH-Dependent Binding between Quantum Dots and Bovine Serum Albumin by Fluorescence Correlation Spectroscopy

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