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首页> 外文期刊>The journal of physical chemistry, C. Nanomaterials and interfaces >Protein Conformation Changes Induced by a Novel Organophosphate-Containing Water-Soluble Derivative of a C_(60)Fullerene Nanoparticle
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Protein Conformation Changes Induced by a Novel Organophosphate-Containing Water-Soluble Derivative of a C_(60)Fullerene Nanoparticle

机译：C_（60）富勒烯纳米粒子的新型含有机磷酸盐的水溶性衍生物诱导的蛋白质构象变化。

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Water-soluble fullerene derivatives have attracted great attention in biological and medical applications.In particular,for any potential in vivo application,the interaction of water-soluble fullerene nanoparticles with human serum albumin(HSA)is crucial.In this study,we synthesized a novel organophosphate-containing water-soluble derivative of C_(60)(C_(60)O_m(OH)_n(C(PO3Et2)2)z(m ≈ 8,n ≈ 12,and l≈ 1),abbreviated as TEMDP-CF).To explore the influence of an organophosphate-containing water-soluble derivative of C_(60)nanoparticles on the conformational changes of HSA,we have investigated the interaction of TEMDP-CF with HSA by biophysical methods,mainly ~(31)P NMR,MALDI-TOF mass spectroscopy,fluorescence,fluorescence dynamics,UV spectroscopy,FT-IR,and CD,for the first time.~(31)P NMR and MALDI-TOF MS analysis have proven the formation of the HSA-TEMDP-CF complex,which is further confirmed by fluorescence and fluorescence dynamics results.We observed a quenching of fluorescence of HSA in the presence of TEMDP-CF and also analyzed the quenching results using the modified Stern-Volmer equation,and a red shift in the emission maximum wavelength can be explained as the result of changes in the ternary structure near the binding site.From fluorescence,fluorescence dynamics,and energy transfer experiment parameters,we can predict the possible binding position of TEMDP-CF on the HSA at the site of subdomain HA,which also agrees with the reported literature.Most significantly,the percentage of the HSA alpha-helix and beta-sheet structure increased,and the beta-turn structure decreased in the CD and FTIR analysis results,revealing that the protein becomes more compact upon association with TEMDP-CF.Furthermore,the increase of the alpha-helix amount,at least on the structure of HSA,may ascribe to the distinct property of the water-soluble TEMDP-CF nanoparticles.
机译：水溶性富勒烯衍生物在生物学和医学应用中引起了广泛的关注。特别是，对于任何潜在的体内应用，水溶性富勒烯纳米粒子与人血清白蛋白（HSA）的相互作用至关重要。 C_（60）（C_（60）O_m（OH）_n（C（PO3Et2）2）z（m≈8，n≈12和l≈1）的新型含有机磷酸盐的水溶性衍生物，简称TEMDP-为了研究含C_（60）纳米粒子的有机磷酸盐的水溶性衍生物对HSA构象变化的影响，我们通过生物物理方法研究了TEMDP-CF与HSA的相互作用，主要是〜（31）P NMR，MALDI-TOF质谱，荧光，荧光动力学，紫外光谱，FT-IR和CD首次出现。〜（31）P NMR和MALDI-TOF MS分析证明了HSA-TEMDP-的形成CF络合物，其荧光和荧光动力学结果进一步证实。我们观察到HSA i的荧光猝灭在存在TEMDP-CF的情况下，还使用修正的Stern-Volmer方程分析了淬灭结果，并且可以解释发射最大波长的红移是结合位点附近三元结构变化的结果。通过荧光动力学和能量转移实验参数，我们可以预测TEMDP-CF在HA子域HA部位与HSA的可能结合位置，这也与报道的文献相吻合。最重要的是，HSAα-螺旋和CD和FTIR分析结果显示β-sheet结构增加，β-turn结构减少，这表明与TEMDP-CF结合后，蛋白质变得更致密。此外，至少在HSA的结构可能归因于水溶性TEMDP-CF纳米颗粒的独特性质。

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