Size-dependent binding of pristine fullerene (nC 60 ) nanoparticles to bovine/human serum albumin

Fu, Xiuwei; Fang, Yingli; Zhao, Hailong; Liu, Shufang

doi:10.1016/j.molstruc.2018.04.067

Cited by 13 publications

(11 citation statements)

References 23 publications

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“…In our previous work, in order to eliminate other factors of the interaction, we obtained nC 60 with different particle sizes by the centrifugation method, and confirmed the size-dependent binding of pristine nC 60 to human serum albumin (HSA)/bovine serum albumin (BSA) by fluorescence quenching spectroscopy [ 13 ]. However, the binding details and mechanism need to be further discussed.…”

Section: Introductionmentioning

confidence: 78%

“…In previous studies, we used the fluorescence method to study the interaction between nC 60 and several proteins. It was found that nC 60 can quench the fluorescence of proteins (BSA and HSA) with a dose–response relationship, and the smaller the particle size of nC 60 , the stronger its ability to quench protein fluorescence [ 13 ]. However, by scanning the UV absorption spectrum of nC 60 and the fluorescence emission spectrum of protein (BSA and HSA, λex = 280 nm), there was an overlap between them ( Figure 1 ).…”

Section: Resultsmentioning

confidence: 99%

“…This means that nC 60 might have absorbed the excitation light and the emission light of the proteins, the so-called fluorescence internal filtering phenomenon, and thus, the fluorescence intensity of the proteins decreased. Due to the low concentration ranges and the weak absorbance of the nC 60 nanoparticles in the experiment, the effect of the fluorescence inner filter on the size-dependent binding law of nC 60 to the proteins was small and can be neglected [ 13 ]. However, to calculate the binding constant and the number of binding sites of the interaction between nC 60 and the proteins, and to comprehend the mechanism of the interaction, the influence of the inner filter had to be considered and deducted.…”

Section: Resultsmentioning

confidence: 99%

“…Stock aqueous dispersion of nC 60 nanoparticles and nC 60 dispersions with different particle size distributions were prepared by the centrifugal method according to our previously published work [ 13 ]. According to the different centrifugal velocities, 5 nC 60 dispersions with different particle sizes were finally obtained and named S 4b , S 0 , S 4 , S 8 , and S 12 , and the average size distributions of 5 dispersions was in the order of S 4b > S 0 > S 4 > S 8 > S 12 (S 4b : 140–160 nm, S 0 : 120–140 nm, S 4 : 90–110 nm, S 8 : 50–70 nm, and S 12 : 30–50 nm) [ 13 ].…”

Section: Experimental Methodsmentioning

confidence: 99%

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Investigating the Size-Dependent Binding of Pristine nC60 to Bovine Serum Albumin by Multi-Spectroscopic Techniques

2021

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The morphology of nanomaterials may affect their interaction with biomacromolecules such as proteins. Previous work has studied the size-dependent binding of pristine nC60 to bovine/human serum albumin using the fluorometric method and found that the fluorescence inner filter effect might affect this interaction. However, if it is necessary to accurately calculate and obtain binding information, the fluorescence inner filter effect should not be ignored. This work aimed to further investigate the effect of the fluorescence inner filter on the interaction between pristine nC60 with different particle sizes (140–160, 120–140, 90–110, 50–70, and 30–50 nm) and bovine serum albumin for a more accurate comprehension of the binding of pristine nC60 to bovine serum albumin. The nC60 nanoparticles with different size distributions used in the experiments were obtained by the solvent displacement and centrifugation method. UV-Vis spectroscopy and fluorescence spectroscopy were used to study the binding of nC60 with different size distributions to bovine serum albumin (BSA) before and after eliminating the fluorescence inner filter effect. The results showed that the fluorescence inner filter effect had an influence on the interaction between nC60 and proteins to some extent, and still did not change the rule of the size-dependent binding of nC60 nanoparticles to BSA. Further studies on the binding parameters (binding constants and the number of binding sites) between them were performed, and the effect of the binding on BSA structures and conformation were also speculated.

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Section: Introductionmentioning

confidence: 78%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Experimental Methodsmentioning

confidence: 99%

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Investigating the Size-Dependent Binding of Pristine nC60 to Bovine Serum Albumin by Multi-Spectroscopic Techniques

2021

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“…44,45 Therefore, it can be speculated that NP size distribution might be the key factor leading to different binding affinities of NPs to serum proteins. 46 In the cellular investigations, it was revealed that NGOs stimulated cytotoxicity in a concentration-dependent manner. The probable mechanism of cytotoxicity was suggested to be triggered by ROS production, cell cycle arrest, and apoptosis induction through the BAX and BCL2 pathway.…”

Section: Discussionmentioning

confidence: 99%

Biophysical, bioinformatical, cellular, and molecular investigations on the effects of graphene oxide nanosheets on the hemoglobin structure and lymphocyte cell cytotoxicity

Babadaei¹,

Moghaddam²,

Solhvand³

et al. 2018

IJN

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BackgroundImplementations of nanoparticles have been receiving great interest in medicine and technology due to their unique characteristics. However, their toxic impacts on the biological system are not well explored.AimThis study aims to investigate the influence of fabricated nano graphene oxide (NGO) sheets on the secondary and quaternary structural alterations of human hemoglobin (Hb) and cytotoxicity against lymphocyte cells.Materials and methodsDifferent spectroscopic methods, such as extrinsic and synchronous fluorescence spectroscopy and far circular dichroism (CD) spectroscopy, molecular docking investigation, cellular assays (trypan blue exclusion, cellular uptake, ROS, cell cycle, and apoptosis), and molecular assay (fold changes in anti/proapoptotic genes [B-cell lymphoma-2 {BCL2}/BAX] expression levels) were used in this study.ResultsTransmission electron microscopy, X-ray diffraction, Fourier transform infrared spectroscopy, and zeta potential investigations revealed the nano-sized nature of NGOs with good colloidal stability. Extrinsic fluorescence spectroscopy by using 8-anilinonaphthalene-1 -sulfonic acid and synchronous fluorescence spectroscopy showed that NGOs can unfold the quaternary structure of Hb in the vicinity of Tyr residues. The CD investigation demonstrated that the α-helicity of Hb experienced substantial alteration upon interaction with increasing concentrations of NGOs. The molecular docking study showed that NGOs interacted with polar residues of Hb. Cellular and molecular assays revealed that NGOs lead to ROS formation, cell cycle arrest, and apoptosis through the BAX and BCL2 pathway.ConclusionThese data reveal that NGOs can induce some protein structural changes and stimulate cytotoxicity against normal cell targets. Therefore, their applications in healthy systems should be limited.

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Multispectroscopic studies on the molecular interactions between bovine γ‐globulin and borohydride‐capped silver nanoparticles

et al. 2022

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Interactions between bovine γ-globulin (BGG) and borohydride-capped silver nanoparticles (BAgNPs) were studied using dynamic light scattering (DLS) and spectroscopic techniques such as UV-vis spectroscopy, fluorescence, and circular dichroism. The results were compared with earlier reported interactions between γ-globulin and citrate-coated AgNPs (CAgNPs). BAgNPs were synthesized and characterized. Irrespective of the coating onAgNPs, nanoparticles had formed ground-state complexes with the protein. CAgNPs, as well as BAgNPs had caused static quenching of tryptophan (Trp) fluorescence of the protein. The change in the capping agent from citrate to borohydride weakened the binding of nanoparticles with the protein. But the same change in capping agent had increased the fluorescence quenching efficiency of AgNPs. Hydrogen bonding and van der Waals interactions were involved in BGG-BAgNPs complex similar to the CAgNPs complex with γ-globulin. Polarity of the Trp microenvironment in BGG was not altered using BAgNPs as opposed to CAgNPs, as supported using synchronous and three-dimensional fluorescence. Resonance light scattering experiments also suggested nano-bio conjugation. Far-UV and near-UV circular dichroism (CD) spectra respectively pointed towards changes in the secondary and tertiary structure of BGG by BAgNPs, which was not observed for CAgNPs.

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Size-dependent binding of pristine fullerene (nC 60 ) nanoparticles to bovine/human serum albumin

Cited by 13 publications

References 23 publications

Investigating the Size-Dependent Binding of Pristine nC60 to Bovine Serum Albumin by Multi-Spectroscopic Techniques

Investigating the Size-Dependent Binding of Pristine nC60 to Bovine Serum Albumin by Multi-Spectroscopic Techniques

Biophysical, bioinformatical, cellular, and molecular investigations on the effects of graphene oxide nanosheets on the hemoglobin structure and lymphocyte cell cytotoxicity

Multispectroscopic studies on the molecular interactions between bovine γ‐globulin and borohydride‐capped silver nanoparticles

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