Size-dependent CdSe quantum dot–lysozyme interaction and effect on enzymatic activity

Das, Kishan; Rawat, Kamla; Patel, Rajan; Bohidar, H. B.

doi:10.1039/c6ra07368a

Cited by 32 publications

(27 citation statements)

References 69 publications

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“…To the best of our knowledge, the toxicity mechanisms of QDs have gradually been explored by the scientists, however, different synthetic methods of QDs own different properties, thus the results of present studies are not enough. Although the interaction between CdTe QDs and lysozyme has been investigated by spectroscopic and microscopy methods, but the inner filter effect was not considered and little work has been done about the isothermal titration calorimetry (ITC) experiment, which is an accepted method among all the available techniques to measure the thermodynamic parameters of the interactions.…”

Section: Introductionmentioning

confidence: 94%

Exploring the influence of MPA‐capped CdTe quantum dots on the structure and function of lysozyme probing by spectroscopic and calorimetric methods

Zhao

Sun

Zhang

et al. 2017

J Biochem & Molecular Tox

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The effect of 3-mercaptopropionic acid (MPA)-capped CdTe quantum dots (QDs) on lysozyme was systematically investigated by spectroscopic methods, enzyme activity assay, and calorimetry techniques. Results show that the MPA-capped CdTe QDs binded to lysozyme through van der Walls forces and hydrogen bondings, causing the decrement of -helical content (∼7%) and increment of -sheet content (∼11%) of lysozyme. The binding caused static quenching of the fluorescence, while the microenvironment of aromatic amino acid residues did not show any significant alteration. The lysozyme activity was affected by the increasing exposure of QDs, it was inhibited to 53.77% under a 6 × 10 −7 M exposure compared with the control group. This work will provide direct evidence about enzyme toxicity of QDs to lysozyme in vitro.

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Section: Introductionmentioning

confidence: 94%

Exploring the influence of MPA‐capped CdTe quantum dots on the structure and function of lysozyme probing by spectroscopic and calorimetric methods

Zhao

Sun

Zhang

et al. 2017

J Biochem & Molecular Tox

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“…In regards to single enzyme systems, recent work with phosphotriesterase (PTE) assembled to CdSe/ZnS core/shell QDs, which emitted at either 525 nm (4.3 ± 0.5 nm diameter) or 625 nm (9.2 ± 0.8 nm diameter) demonstrated that both QDs significantly enhanced immobilized enzymatic activity compared to enzyme in free solution; the k cat increased~4-fold while the enzymatic efficiency (k cat /K M ) increased 2-fold [82]. Although the focus of this review is exclusively on the enhancement of enzymatic activity with enzymes immobilized to QDs, we note that several reports have also indicated striking improvements in enzymatic activity when the substrate is attached to QDs, particularly as proteolytic reporters [87,88,90,[95][96][97][98][99][100][101][102][103][104][105][106][107].…”

Section: Enzyme Immobilization On Qdsmentioning

confidence: 92%

Quantum Dots and Gold Nanoparticles as Scaffolds for Enzymatic Enhancement: Recent Advances and the Influence of Nanoparticle Size

et al. 2020

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Nanoparticle scaffolds can impart multiple benefits onto immobilized enzymes including enhanced stability, activity, and recoverability. The magnitude of these benefits is modulated by features inherent to the scaffold–enzyme conjugate, amongst which the size of the nanoscaffold itself can be critically important. In this review, we highlight the benefits of enzyme immobilization on nanoparticles and the factors affecting these benefits using quantum dots and gold nanoparticles as representative materials due to their maturity. We then review recent literature on the use of these scaffolds for enzyme immobilization and as a means to dissect the underlying mechanisms. Detailed analysis of the literature suggests that there is a “sweet-spot” for scaffold size and the ratio of immobilized enzyme to scaffold, with smaller scaffolds and lower enzyme:scaffold ratios generally providing higher enzymatic activities. We anticipate that ongoing studies of enzyme immobilization onto nanoscale scaffolds will continue to sharpen our understanding of what gives rise to beneficial characteristics and allow for the next important step, namely, that of translation to large-scale processes that exploit these properties.

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“…Nanomaterials such as silica, Ag, Au, and semiconductor QDs such as ZnO and CdSe have been found to alter the biological activity of the enzymes by significantly impacting their structure (Vertegel et al 2004;Secundo 2013;Petkova et al 2012;Zhao et al 2019;Das et al 2016). Zhao et al (2019) investigated the interaction of MPA-CdSe/ZnS with catalase(CAT) and superoxide dismutase (SOD) within hepatocytes of mice and found that hydrophobic force was involved in MPA-CdSe/ZnS binding to CAT and SOD, the primary consequence of which was an alteration in the secondary structure of enzymes (reduction in the α-helix content) (Zhao et al 2019).…”

Section: Introductionmentioning

confidence: 99%

Size-responsive differential modulation in α-amylase by MPA-CdSe QDs: multispectroscopy and molecular docking study

2021

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in dose-and size-dependent manner. Effect on α-amylase activity in complex form with size varied CdSe QDs suggested higher inhibition of enzymatic activity by smaller size QDs as compared to larger size. Molecular docking of MPA ligand with α-amylase revealed that interaction was majorly driven by hydrophobic forces. It further suggested that MPA did not interact with active site of α-amylase, thus acting as non-competitive inhibitor. The study thus involved a comprehensive analysis of the structural and functional modulation in α-amylase by interaction with hydrophilic MPAcapped CdSe QDs of different sizes.

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Size-dependent CdSe quantum dot–lysozyme interaction and effect on enzymatic activity

Abstract: Size-dependent (2.5 and 6.3 nm) interaction of MPA modified hydrophilic CdSe quantum dots with lysozyme are reported.

Cited by 32 publications

References 69 publications

Exploring the influence of MPA‐capped CdTe quantum dots on the structure and function of lysozyme probing by spectroscopic and calorimetric methods

Exploring the influence of MPA‐capped CdTe quantum dots on the structure and function of lysozyme probing by spectroscopic and calorimetric methods

Quantum Dots and Gold Nanoparticles as Scaffolds for Enzymatic Enhancement: Recent Advances and the Influence of Nanoparticle Size

Size-responsive differential modulation in α-amylase by MPA-CdSe QDs: multispectroscopy and molecular docking study

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