Dual effects of fibrinogen decoration on the tuning of silica nanoparticles-induced autophagic response: The implication of sedimentation and internalization

Zhang, Lihui; Wei, Wei; Liu, Zixuan; Liu, Xuting; Song, Erqun; Song, Yang

doi:10.1016/j.jhazmat.2020.124467

Cited by 6 publications

(5 citation statements)

References 52 publications

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“…CD spectra were determined by a CD spectrometer (MOS-450, BioLogic, France). The CD spectral data were normalized as molar residue ellipticity, and the secondary structure of each protein (helix, β-sheet, turn, and random coil) was obtained using the online analysis software DichroWeb …”

Section: Methodsmentioning

confidence: 99%

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Mechanistic Insights of TiO₂ Nanoparticles with Different Surface Charges on Aβ₄₂ Peptide Early Aggregation: An In Vitro and In Silico Study

Wen

Yan

et al. 2023

Langmuir

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Humans may intendedly or unintendedly be exposed to nanomaterials through food, water, and air. Upon exposure, nanomaterials can pierce the bloodstream and translocate to secondary organs, including the brain, which warrants increased concern for the potential health impacts of nanomaterials. Due to their large surface area and interaction energy, nanomaterials can adsorb surrounding proteins. The misfolding and self-aggregation of amyloid-β (Aβ) have been considered significant factors in the pathogenesis of Alzheimer's disease. We thus hypothesize that braintargeted nanomaterials may modulate Aβ aggregation and cause related neurotoxicity. Here, we showed that TiO 2 nanoparticles (NPs) and their aminated analogue (TiO 2 -NH 2 NPs) adsorb the Aβ 42 peptide and accelerate its early oligomerization. Molecular dynamics simulation indicated that the adsorption onto TiO 2 NPs and TiO 2 -NH 2 NPs surfaces can stabilize the β-sheet-rich conformations formed by the Aβ 42 peptide. The binding sites between TiO 2 -NH 2 NPs and the Aβ 42 oligomer surface were mainly concentrated in the hydrophobic core region, and the β-sheet conformation spontaneously formed by Aβ 42 oligomers can be better stabilized through a hydrogen bond, electrostatic attraction, and hydrophobic interaction. This study will further help in the understanding of nanomaterial-related neurotoxicities and the regulation of their applications.

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Section: Methodsmentioning

confidence: 99%

“…The CD spectral data were normalized as molar residue ellipticity, and the secondary structure of each protein (helix, β-sheet, turn, and random coil) was obtained using the online analysis software DichroWeb. 51 AFM. Aβ 42 solution (20 μM) was mixed with 40 μg/mL NPs in a shaking incubator at 37 °C.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

Mechanistic Insights of TiO₂ Nanoparticles with Different Surface Charges on Aβ₄₂ Peptide Early Aggregation: An In Vitro and In Silico Study

Wen

Yan

et al. 2023

Langmuir

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“…Furthermore, van der Waals interactions serve to maintain the folded configuration of a protein. Therefore, when proteins approach a surface, adsorption forces governing proteinsurface interactions can easily disrupt these non-covalent interactions in the protein structure, resulting in conformational changes or the collapse of protein structureunfolding 31,32 (Fig. 1).…”

Section: Biological Factors That Influence Protein Corona Conformatio...mentioning

confidence: 99%

“…The interaction of BSA, Hb, and FBG with SiO 2 NPs does not significantly change the secondary structure of adsorbed FBG, while the secondary structure of BSA and Hb changes with the increasing amount of SiO 2 NPs, which leads to the loosening and unfolding of their structures. 32 Furthermore, in contrast to BSA and Hb, FBG adsorption on SiO 2 NPs delays the autophagy-inducing activity in HUVECs cells by stabilizing SiO 2 NPs, preventing their sedimentation and cellular internalization. However, the protective effect of FBG only works for non-phagocytic cells and is limited to 24 h.…”

Section: B Silica Nanoparticlesmentioning

confidence: 99%

Nanoparticle protein corona: from structure and function to therapeutic targeting

et al. 2023

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“…However, it has been demonstrated that even with antifouling polymer coatings, the non-specific protein adsorption on the surface of NMs is inevitable [ 9 ]. Recent studies have shown that precoating using endogenous biomolecules, such as albumin, clusterin, and fibrinogen, has emerged as a promising strategy [ 10 , 11 ]. Preformed albumin–Au nanorod complexes have been demonstrated to reduce cytotoxicity and macrophage uptake, promote biostability and long circulation time, and enhance tumor targeting and penetration [ 12 ].…”

Section: Introductionmentioning

confidence: 99%

Bi-Functionalized Transferrin@MoS2-PEG Nanosheets for Improving Cellular Uptake in HepG2 Cells

Liang

Wang

et al. 2023

Materials

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Pre-coating with a protein corona on the surface of nanomaterials (NMs) is an important strategy for reducing non-specific serum protein absorption while maintaining targeting specificity. Here, we present lipoic acid-terminated polyethylene glycol and transferrin bi-functionalized MoS2 nanosheets (Tf@MoS2-PEG NSs) as a feasible approach to enhance cellular uptake. Tf@MoS2-PEG NSs can maintain good dispersion stability in cell culture medium and effectively protect MoS2 NSs from oxidation in ambient aqueous conditions. Competitive adsorption experiments indicate that transferrin was more prone to bind MoS2 NSs than bovine serum albumin (BSA). It is noteworthy that single HepG2 cell uptake of Tf@MoS2-PEG presented a heterogeneous distribution pattern, and the cellular uptake amount spanned a broader range (from 0.4 fg to 2.4 fg). Comparatively, the intracellular Mo masses in HepG2 cells treated with BSA@MoS2-PEG and MoS2-PEG showed narrower distribution, indicating homogeneous uptake in the single HepG2 cells. Over 5% of HepG2 cells presented uptake of the Tf@MoS2-PEG over 1.2 fg of Mo, about three-fold that of BSA@MoS2-PEG (0.4 fg of Mo). Overall, this work suggests that Tf coating enhances the cellular uptake of MoS2 NSs and is a promising strategy for improving the intracellular uptake efficiency of cancer cells.

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Dual effects of fibrinogen decoration on the tuning of silica nanoparticles-induced autophagic response: The implication of sedimentation and internalization

Cited by 6 publications

References 52 publications

Mechanistic Insights of TiO₂ Nanoparticles with Different Surface Charges on Aβ₄₂ Peptide Early Aggregation: An In Vitro and In Silico Study

Mechanistic Insights of TiO₂ Nanoparticles with Different Surface Charges on Aβ₄₂ Peptide Early Aggregation: An In Vitro and In Silico Study

Nanoparticle protein corona: from structure and function to therapeutic targeting

Bi-Functionalized Transferrin@MoS2-PEG Nanosheets for Improving Cellular Uptake in HepG2 Cells

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Dual effects of fibrinogen decoration on the tuning of silica nanoparticles-induced autophagic response: The implication of sedimentation and internalization

Cited by 6 publications

References 52 publications

Mechanistic Insights of TiO2 Nanoparticles with Different Surface Charges on Aβ42 Peptide Early Aggregation: An In Vitro and In Silico Study

Mechanistic Insights of TiO2 Nanoparticles with Different Surface Charges on Aβ42 Peptide Early Aggregation: An In Vitro and In Silico Study

Nanoparticle protein corona: from structure and function to therapeutic targeting

Bi-Functionalized Transferrin@MoS2-PEG Nanosheets for Improving Cellular Uptake in HepG2 Cells

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Product

Resources

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Mechanistic Insights of TiO₂ Nanoparticles with Different Surface Charges on Aβ₄₂ Peptide Early Aggregation: An In Vitro and In Silico Study

Mechanistic Insights of TiO₂ Nanoparticles with Different Surface Charges on Aβ₄₂ Peptide Early Aggregation: An In Vitro and In Silico Study