Romanian Academy, Institute of Physical Chemistry "Ilie Murgulescu", Splaiul Independentei 202, 060021 Bucharest, Romania.
Department of Physical Chemistry, University of Bucharest, Bd Regina Elisabeta 4-12, Bucharest 030018, Romania.
Spectrochim Acta A Mol Biomol Spectrosc. 2017 Jan 5;170:1-8. doi: 10.1016/j.saa.2016.06.039. Epub 2016 Jun 29.
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.
采用荧光和拉曼光谱法研究了 3-羟基黄酮与血清蛋白(BSA 和 HSA)在卵磷脂脂质双层(PC)与银纳米粒子(SNPs)相互作用。通过解卷积算法对 BSA 二级结构进行定量分析,表明当脂质加入溶液中时,α-螺旋结构减少。讨论了温度对激发态分子内质子转移速率和 3-HF 在 HSA/PC/SNPs 体系中双荧光发射的影响。还研究了 3-HF 在 HSA/PC/SNPs 体系中的抗氧化活性。在 SNPs 的存在下,3-HF 的抗氧化活性降低。讨论结果与蛋白质的二级结构以及基于 3-HF 的纳米系统与有用的在氧化应激过程中的局部制剂相关。