ArticleHeliyon2023
Effects of black cumin-based antimalarial drug loaded with nano-emulsion of bovine and human serum albumins by spectroscopic and molecular docking studies.
Article in Heliyon, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 17 citations in OpenAlex.
- Synthesis, Photophysical Properties and Antioxidant Activity of Novel Quinoline Derivatives.Journal of fluorescence · 2025Article
- Interaction mechanism of oseltamivir phosphate with bovine serum albumin: multispectroscopic and molecular docking study.BMC chemistry · 2024Article
- Article
- Recent Updates on Interaction Studies and Drug Delivery of Antimalarials with Serum Albumin Proteins.Current medicinal chemistry · 2024Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The growing understanding of nanoemulsion biomedical applications necessitates a basic understanding of protein-drug-loaded nanoemulsion interaction. In our present study, we investigated the binding interactions of Mefloquine (MEF)-loaded black cumin seed oil (Thymoquinone) nanoemulsion of different concentrations towards human and bovine serum albumin (HSA&BSA).Fluorescenceemission,three-dimensionalspectra,UV-visible spectroscopy, and FTIR-spectroscopy, techniques were used together with molecular docking studies to identify the binding effects. The ground state complex formation between Mefloquine-loaded black cumin seed oil nanoemulsion and protein fluorophores was confirmed by a decrease in fluorescence intensity and disputed hyper-chronicity found in the UV-visible spectra of albumins. According to three-dimensional fluorescence spectral analysis, the addition of MEF in thymoquinone impacted the microenvironment around aromatic amino acid (tryptophan and tyrosine) residues in HSA. The quenching mechanism is determined to be static contact by stern-volmer analysis, resulting in the formation of a stable bioconjugate. Significant modifications in the amide FTIR frequencies at around 1600 cm
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