ArticleThe protein journal2019
Interaction of a Model Hydrophobic Drug Dimethylcurcumin with Albumin Nanoparticles.
Article in The protein journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed.
- Curcumin Bound Seleno-BSA, a Novel Bifunctional Macromolecular Therapeutic System Against A549 Lung Cancer Cells: Photophysical Characterizations, Cellular Uptake, and Efficacy.Chemistry, an Asian journal · 2026Article
- Formulation of PVA Hydrogel Patch as a Drug Delivery System of Albumin Nanoparticles Loaded with Curcumin.Gels (Basel, Switzerland) · 2025Article
- Functionalized albumin nanoparticles: A multifunctional platform for enhanced brain drug delivery.Materials today. Bio · 2025Review
- A Promising Anticancer Agent Dimethoxycurcumin: Aspects of Pharmacokinetics, Efficacy, Mechanism, and Nanoformulation for Drug Delivery.Frontiers in pharmacology · 2021Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aim of present study was to investigate the binding interactions of a model hydrophobic molecule, dimethylcurcumin (DMC) with nanoparticle form of bovine serum albumin (BSA) using fluorescence spectroscopy techniques. For this, BSA nanoparticles (size = 62.0 ± 3.5 nm, molecular weight = 11,243 ± 3445 kD) prepared by thermal denaturation method was mixed with DMC in solution and monitored for fluorescence emission of tryptophan (Trp) residue as well as DMC separately. The emission maximum of DMC in nanoparticles form exhibited more blue sift and quenched the excited state of tryptophan (Trp) by six fold higher than in the native form of BSA. By analyzing Trp fluorescence, the mean binding constant (K) estimated for the interaction of DMC with native and nanoparticles forms of BSA was 2.7 ± 0.4 × 10
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Registered trials
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