ArticleBiomolecules2020
The Interaction of Temozolomide with Blood Components Suggests the Potential Use of Human Serum Albumin as a Biomimetic Carrier for the Drug.
Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 33 citations in OpenAlex.
- Temozolomide-Derived AIC Is Incorporated into Purine Synthesis in Glioblastoma.Chemical research in toxicology · 2025Article
- GLUT3 enhances chemosensitivity in glioblastoma by transporting temozolomide and capecitabine.Cell death discovery · 2025Article
- Article
- Spectroscopic insights into BSA-mediated deaggregation of m-THPC.Scientific reports · 2024Article
- Temozolomide and flavonoids against glioma: from absorption and metabolism to exosomal delivery.Naunyn-Schmiedeberg's archives of pharmacology · 2024Review
- Drug metabolism-related gene ABCA1 augments temozolomide chemoresistance and immune infiltration abundance of M2 macrophages in glioma.European journal of medical research · 2023Article
- Insight into the interaction between tannin acid and bovine serum albumin from a spectroscopic and molecular docking perspective.RSC advances · 2023Article
- Glioblastoma-Derived Small Extracellular Vesicles: Nanoparticles for Glioma Treatment.International journal of molecular sciences · 2023Article
- Dissecting the Interactions between Chlorin e6 and Human Serum Albumin.Molecules (Basel, Switzerland) · 2023Article
- Carrying Temoporfin with Human Serum Albumin: A New Perspective for Photodynamic Application in Head and Neck Cancer.Biomolecules · 2022Article
- CD, UV, and In Silico Insights on the Effect of 1,3-Bis(1'-uracilyl)-2-propanone on Serum Albumin Structure.Biomolecules · 2022Article
- Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The interaction of temozolomide (TMZ) (the main chemotherapeutic agent for brain tumors) with blood components has not been studied at the molecular level to date, even though such information is essential in the design of dosage forms for optimal therapy. This work explores the binding of TMZ to human serum albumin (HSA) and alpha-1-acid glycoprotein (AGP), as well as to blood cell-mimicking membrane systems. Absorption and fluorescence experiments with model membranes indicate that TMZ does not penetrate into the lipid bilayer, but binds to the membrane surface with very low affinity. Fluorescence experiments performed with the plasma proteins suggest that in human plasma, most of the bound TMZ is attached to HSA rather than to AGP. This interaction is moderate and likely mediated by hydrogen-bonding and hydrophobic forces, which increase the hydrolytic stability of the drug. These experiments are supported by docking and molecular dynamics simulations, which reveal that TMZ is mainly inserted in the subdomain IIA of HSA, establishing π-stacking interactions with the tryptophan residue. Considering the overexpression of albumin receptors in tumor cells, our results propose that part of the administered TMZ may reach its target bound to plasma albumin and suggest that HSA-based nanocarriers are suitable candidates for designing biomimetic delivery systems that selectively transport TMZ to tumor cells.
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Registered trials
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