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Collagen-Catechin Interactions: a NMR Approach

机译:胶原蛋白儿茶素相互作用:NMR方法

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This work focuses on understanding at molecular level the mechanism of interaction between collagen and catechin. Interactions were investigated by NMR measurements both in solution and in solid state. We also explored the possibilities offered by NMR to characterize the effect of catechin on the stability of collagen to oxidation. Collagen type I fibres were used throughout the study. Collagen was treated with two different concentration of catechin . Oxidation was carried out by incubation of collagen solution with three different oxidation system s (Fe(Ⅱ)/H_2O_2; Cu(Ⅱ)/H_2O_3; NaOCl/H_2O_2). High resolution 1-H 1D and 2D spectroscopy were recorded at 30°C on Bruker Avance 400. Solid state NMR experiments were performed by a Bruker spectrometer equipped with a CPS MAS accessory. Data obtained from 1D and 2 D proton NMR and ~(13)C CP MAS spectroscopy pointed out that interactions between collagen and catechin preferentially occurred between catechin B ring and the amino acids proline and hydroxyproline. Oxidation studies carried out by metal/H2O2 systems on collagen showed that both iron and copper were able to interact with collagen by site specific attak.A strong effect of catechin in collagen complex was shown. Catechin was able to protect collagen proline from oxidation by metal/H_2O_2 systems. The protective effect of catechin towards collagen oxidation was markedly evident for the copper oxidation system.
机译:这项工作侧重于在分子水平上了解胶原蛋白与儿茶素之间相互作用的机理。通过在溶液和固态下的NMR测量研究了相互作用。我们还探索了NMR提供的可能性,以表征儿茶素对胶原蛋白氧化稳定性的影响。在整个研究过程中都使用了I型胶原纤维。用两种不同浓度的儿茶素处理胶原蛋白。通过将胶原溶液与三种不同的氧化系统(Fe(Ⅱ)/ H_2O_2; Cu(Ⅱ)/ H_2O_3; NaOCl / H_2O_2)孵育进行氧化。在Bruker Avance 400上于30°C记录高分辨率的1-H 1D和2D光谱。通过配备CPS MAS附件的Bruker光谱仪进行固态NMR实验。从1D和2D质子NMR和〜(13)C CP MAS光谱获得的数据指出,胶原蛋白和儿茶素之间的相互作用优先发生在儿茶素B环与氨基酸脯氨酸和羟脯氨酸之间。金属/过氧化氢对胶原蛋白的氧化研究表明,铁和铜都可以通过位点特异性结合与胶原蛋白相互作用。显示儿茶素在胶原蛋白复合物中具有很强的作用。儿茶素能够保护脯氨酸胶原蛋白免受金属/ H_2O_2系统的氧化。儿茶素对胶原氧化的保护作用对于铜氧化系统是明显的。

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