ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2019
Perturbation of tubulin structure by stellate gold nanoparticles retards MDA-MB-231 breast cancer cell viability.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 13 citations in OpenAlex.
- Tryptone-stabilized silver nanoparticles' potential to mitigate planktonic and biofilm growth forms of Serratia marcescens.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023Article
- Gold Nanoparticles in Triple-Negative Breast Cancer Therapeutics.Current medicinal chemistry · 2023Review
- Use of Nanoparticles in Delivery of Nucleic Acids for Melanoma Treatment.Methods in molecular biology (Clifton, N.J.) · 2021Article
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Authors and funding
4 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Gold nanoparticles (GNPs) of different sizes and shapes have been investigated extensively for their therapeutic potential against several diseases including cancer. However, the mechanisms with which they affect the cells are yet to be fully comprehended. In this study, we report the strong antiproliferative potential of novel, star-shaped ("stellate") GNPs that target tubulin-the building-block protein of the cytoskeletal filaments called microtubules-and disrupt microtubule network integrity. The stellate GNPs ("sGNPs") were synthesized from tryptone-stabilized GNPs ("tGNPs") and characterized by various spectroscopy methods combined with high-resolution transmission electron microscopy. Among a panel of cancer cell lines tested, they showed strong antiproliferative and anti-clonogenic efficacy against MDA-MB-231 cells. The antiproliferative mechanism of the sGNPs involves perturbation of the secondary and tertiary conformation of tubulin as evidenced by far-UV circular dichroism and anilinonaphthalene sulphate-binding assays. The structural perturbation of tubulin retarded its assembly competence as evidenced by polymer mass analysis and electron microscopy imaging of tubulin assembled in vitro and by immunofluorescence visualization of the cellular microtubules. The treated cells also induced cell cycle arrest at G1 phase. Taken together, our data suggest that sGNPs are potent, tubulin-targeted antiproliferative particles that can be evaluated further for their anticancer potential.
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