Interactions between carbon nanodots with human serum albumin and γ-globulins: The effects on the transportation function

Xu, Ziqiang; Yang, Qiqi; Lan, Jiayi; Zhang, Jiaqi; Wu, Peng; Jin, Jian-Cheng; Jiang, Feng-Lei; Liu, Yi

doi:10.1016/j.jhazmat.2015.08.062

Cited by 107 publications

(50 citation statements)

References 39 publications

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“…Samples of all PEGylated NPs exhibited an insignificant change in HSA maximum fluorescence intensity ( P > 0.05) as illustrated in Figure . Notably, there was no obvious shift in maximum emission wavelength, indicating that NPs have little influence on the microenvironment of tryptophan residue . For all samples, the maximum emission wavelength was 320 nm.…”

Section: Resultsmentioning

confidence: 90%

“…Proton ( 1 H) NMR was used to quantify PEG on the NPs . Briefly, 5 mg of lyophilized NPs was weighed and dissolved in deuterated chloroform (CDCl 3 ) containing 1% (w/w) hexadeuterodimethyl sulfoxide (TMS) as an internal standard.…”

Section: Methodsmentioning

confidence: 99%

“…Proton ( 1 H) NMR was used to quantify PEG on the NPs. [25] Briefly, 5 mg of lyophilized NPs was weighed and dissolved in deuterated chloroform (CDCl 3 ) containing 1% (w/w) hexadeuterodimethyl sulfoxide (TMS) as an internal standard. [1] H NMR analysis was performed using a Bruker 400 REM instrument running at 400 mHz with relaxation time set at 10 s and ZG at 90°.…”

Section: Determination Of Np Peg Contentmentioning

confidence: 99%

“…Notably, there was no obvious shift in maximum emission wavelength, indicating that NPs have little influence on the microenvironment of tryptophan residue. [25] For all samples, the maximum emission wavelength was 320 nm. The protein binding behaviour of non-PEGylated NPs was significantly greater than that of all PEGylated NPs, as illustrated in Figure 6.…”

Section: Np Stability In Human Serummentioning

confidence: 99%

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Influence of PEGylation on PLGA nanoparticle properties, hydrophobic drug release and interactions with human serum albumin

Samkange

D’Souza

Obikeze

et al. 2019

Journal of Pharmacy and Pharmacology

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Objective To evaluate the impact of PEG content on poly(lactic‐co‐glycolic acid) (PLGA) NP physicochemical properties, hydrophobic drug release (rifampicin as a model drug) and human serum protein binding. Methods Rifampicin loaded and unloaded nanoparticles with PEG content of 0–17% (w/w) were prepared by an emulsification–evaporation technique. Nanoparticles were characterized for size, zeta potential and morphology. PEGlyation was confirmed using proton nuclear magnetic resonance (1H NMR). Fluorescence spectroscopy and dynamic light scattering were used to determine nanoparticle‐protein binding, binding constants and stability of nanoparticles in human serum, respectively. Drug loading and release were determined by UV‐VIS spectroscopy and drug release data was mathematically modelled. Key findings A NP PEG content of 17% w/w significantly retarded release of rifampicin from PLGA NPs and altered kinetics of drug release. Stern–Volmer (Ksv) protein binding constants decreased upon PEG incorporation. A 2% w/w PEG was sufficient to significantly reduce protein binding extent to PLGA NPs and maintain particle size distributions. Conclusion The ability to fine tune drug release and formation of protein corona around nanoparticles is crucial to formulation scientists. This study suggests that PLGA NPs with low PEG content might be suitable for extended circulation and rapid drug release and that higher PEG content retards hydrophobic drug release.

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Section: Resultsmentioning

confidence: 90%

Section: Methodsmentioning

confidence: 99%

Section: Determination Of Np Peg Contentmentioning

confidence: 99%

Section: Np Stability In Human Serummentioning

confidence: 99%

See 2 more Smart Citations

Influence of PEGylation on PLGA nanoparticle properties, hydrophobic drug release and interactions with human serum albumin

Samkange

D’Souza

Obikeze

et al. 2019

Journal of Pharmacy and Pharmacology

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“…Despite many promising applications in biological research, studies of the interaction between biomolecules and USNPs are still rare in the literature and often controversial. 23 Recently, some studies on the interactions between proteins and USNPs, such as Ag NPs, 17 Au NPs, 9,24,25 carbon-NPs, 26,27 quantum dots, 28 Si NPs 29 and oxide NPs 30 have been reported. They either assumed that the proteins and nanoparticles formed complexes or that they generated different protein coronas, which reflected the strength of the affinity of binding between the constituents.…”

Section: Introductionmentioning

confidence: 99%

Identification of the binding site between bovine serum albumin and ultrasmall SiC fluorescent biomarkers

Dravecz

Jánosi

Beke

et al. 2018

Phys. Chem. Chem. Phys.

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Ultrasmall silicon carbide nanoparticles (SiC USNPs) are very promising biomarkers for developing new applications in diagnostics, cell monitoring or drug delivery, even though their interaction with biological molecules such as different proteins has not yet been investigated in detail. In this study, the biological behaviour of SiC USNPs in a medium modeling a living organism was investigated in detail through the dependence of the fluorescence on interactions between bovine serum albumin (BSA) and SiC USNPs. The interaction shows transient nanoparticle-protein associations due to the restricted diffusion behaviour of the nanoparticles in the vicinity of a protein. The transient association manifests in a complex fluorescence quenching mechanism where the dynamic component was dominated by Förster resonance energy transfer. By studying SiC nanoparticles of different sizes, it can be concluded that the transient effect is an ultrasmall nanoparticle behaviour.

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Rational Design of Nanocarriers for Intracellular Protein Delivery

et al. 2019

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Protein/antibody therapeutics have exhibited the advantages of high specificity and activity even at an extremely low concentration compared to small molecule drugs. However, they are accompanied by unfavorable physicochemical properties such as fragile tertiary structure, large molecular size, and poor penetration of the membrane, and thus the clinical use of protein drugs is hindered by inefficient delivery of proteins into the host cells. To overcome the challenges associated with protein therapeutics and enhance their biopharmaceutical applications, various protein‐loaded nanocarriers with desired functions, such as lipid nanocapsules, polymeric nanoparticles, inorganic nanoparticles, and peptides, are developed. In this review, the different strategies for intracellular delivery of proteins are comprehensively summarized. Their designed routes, mechanisms of action, and potential therapeutics in live cells or in vivo are discussed in detail. Furthermore, the perspective on the new generation of delivery systems toward the emerging area of protein‐based therapeutics is presented as well.

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Interactions between carbon nanodots with human serum albumin and γ-globulins: The effects on the transportation function

Cited by 107 publications

References 39 publications

Influence of PEGylation on PLGA nanoparticle properties, hydrophobic drug release and interactions with human serum albumin

Influence of PEGylation on PLGA nanoparticle properties, hydrophobic drug release and interactions with human serum albumin

Identification of the binding site between bovine serum albumin and ultrasmall SiC fluorescent biomarkers

Rational Design of Nanocarriers for Intracellular Protein Delivery

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