| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1230792 | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy | 2017 | 8 Pages |
•Secondary structure of BSA binding 3-HF into lecithin lipidic bi-layers and immobilized on silver nanoparticles.•Antioxidant activity of 3-HF into lecithin lipidic bi-layers and immobilized on silver nanoparticles.•The results have relevance to the secondary structure of proteins and of the 3-HF based nano-systems, in the oxidative stress process.
The interaction of 3-Hydroxyflavone with serum proteins (BSA and HSA) in lecithin lipidic bi-layers (PC) immobilized on silver nanoparticles (SNPs), was studied by fluorescence and Raman spectroscopy. BSA secondary structure was quantified with a deconvolution algorithm, showing a decrease in α-helix structure when lipids were added to the solution. The effect of temperature on the rate of the excited-state intra-molecular proton transfer and on the dual fluorescence emission of 3-HF in the HSA/PC/SNPs systems was discussed. Evaluation of the antioxidant activity of 3-HF in HSA/PC/SNPs systems was also studied. The antioxidant activity of 3-HF decreased in the presence of SNPs. The results are discussed with relevance to the secondary structure of proteins and of the 3-HF based nano-systems to a topical formulation useful in the oxidative stress process.
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