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Published on: February 21, 2019
Spectroscopic study of 3-Hydroxyflavone - protein interaction in lipidic bi-layers immobilized on silver
Mariana Voicescu1, Sorana Ionescu2, Cristina L Nistor3
1Romanian Academy, Institute of Physical Chemistry "Ilie Murgulescu", Splaiul Independentei 202, 060021 Bucharest, Romania.
Abstract:
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.
