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Figure 1.

Characterization of the AuNP and protein corona made from cell lysates of OSE and OV167.

a) A cartoon showing functionalization of 5 nm gold nanoparticle to create positively charged (+AuNP) or negatively charged (AuNP) gold nanoparticles. b) Amount of protein bound on the nanoparticle as determined by Bradford assay. The binding of protein is evident from the increase in surface size via DLS on c) +AuNP and d) AuNP.

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Table 1.

Dynamic Light Scattering (DLS) to determine hydrodynamic diameter (dH) of AuNPs before and after incubation with OV167 and OSE lysates.

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Table 2.

Zeta Potential in mV of +AuNP and AuNP before and after incubation with the lysates of OV167 and OSE, respectively.

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Figure 2.

Selectivity of the proteins bound to positively charged (+AuNP) vs negatively charged (AuNP) particles.

Venn diagrams show proteins identified in the protein corona around +AuNP and AuNP from a) normal OSE cell lysates and b) malignant OV167 cell lysates. The figure clearly depicts the preferential enrichment of low abundance proteins by engineered nanoparticles that were not detectable in the lysates by proteomics analysis. These proteins, which were otherwise undetected, could potentially be new therapeutic targets.

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Figure 3.

Venn diagram demonstrating the difference between the proteins that make up the corona for a) +AuNP, b) AuNP from the cell lysates and c) the different between proteins in the OV167 and OSE cell lysates.

These differences in the composition of the lysates could be exploited to identify new therapeutic targets in ovarian cancer.

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Figure 4.

Enrichment and functional consequence of HDGF.

a) Western blot confirming the presence of HDGF on +AuNP- corona whereas Hsp90 on AuNP- corona. Also shown is Hsp70 (known to be present in all NP coronas via MS). b) Expression of HDGF in ovarian cell lines. c) Knockdown of HDGF in A2780 cell line using HDGF-siRNAs (KD-siRNA) and compared with the scrambled control (scRNA); d) Effect of silencing HDGF on proliferation of ovarian cancer cells analyzed by [3H]-thymidine incorporation assay.

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