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首页> 外文期刊>Langmuir: The ACS Journal of Surfaces and Colloids >Interaction of Vitamin K-1 and Vitamin K-2 with Dimyristoylphosphatidylcholine and Their Location in the Membrane
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Interaction of Vitamin K-1 and Vitamin K-2 with Dimyristoylphosphatidylcholine and Their Location in the Membrane

机译:维生素K-1和维生素K-2与二巯基磷脂酰胆碱的相互作用及其在膜中的位置

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摘要

Vitamin K-1 and vitamin K-2 play very important biological roles as members of chains of electron transport as antioxidants in membranes and as cofactors for the posttranslational modification of proteins that participate in a number of physiological functions such as coagulation. The interaction of these vitamins with dimyristoylphosphatidylcholine (DMPC) model membranes has been studied by using a biophysical approach. It was observed by using differential scanning calorimetry that both vitamins have a very limited ron miscibility with DMPC and they form domains rich in the vitamins at high concentrations. Experiments using X-ray diffraction also showed the formation of different phases as a kHZ consequence of the inclusion of either vitamin K at temperatures below the phase transition. However, in the fluid state, a homogeneous phase was detected, and a decrease in the thickness of the membrane was accompanied by an increase in the water layer thickness. H-2 NMR spectroscopy showed that both vitamins K induced a decrease in the onset of the phase transition, which was bigger for vitamin K-1, and both vitamins decreased the order of the membrane as seen through the first moment (M-1). H-1 NOESY MAS-NMR showed that protons located at the rings or at the beginning of the lateral chain of both vitamins K interacted with a clear preference with protons located in the polar part of DMPC. On the other hand, protons located on the lateral chain have a nearer proximity with the methyl end of the myristoyl chains of DMPC. In agreement with the H-2 NMR, ATR-FTIR (attenuated total reflectance Fourier transform infrared spectroscopy) indicated that both vitamins decreased the order parameters of DMPC. It was additionally deduced that the lateral chains of both vitamins were oriented almost in parallel to the myristoyl chains of the phospholipid.
机译:维生素K-1和维生素K-2在膜中作为电子传输链作为抗氧化剂的抗氧化剂和作为蛋白质的后期改性的辅助蛋白的辅助蛋白,蛋白质的抗氧化剂的成员具有非常重要的生物学作用。通过使用生物物理方法研究了这些维生素与二硒酰基磷脂酰胆碱(DMPC)模型膜的相互作用。通过使用差示扫描量热法观察,差动扫描量热量与DMPC具有非常有限的RON混溶性,它们在高浓度下富含维生素的结构域。使用X射线衍射的实验还显示出不同相对于在低于相转变的温度下包含维生素K的kHz的结果。然而,在流体状态下,检测均相,膜的厚度的降低伴随着水层厚度的增加。 H-2 NMR光谱显示,维生素K诱导相变的发作减少,这对维生素K-1更大,两种维生素都会降低膜的顺序,如第一时刻(M-1)所示。 H-1 Noesy Mas-NMR显示,位于环的形状或两种维生素K的侧链开始时与位于DMPC的极性部分的质子相互作用。另一方面,位于横向链上的质子与DMPC的Myristoyl链的甲基端近的近距离接近。在H-2 NMR的同意中,ATR-FTIR(衰减的总反射率傅立叶变换红外光谱)表明,两种维生素都降低了DMPC的顺序参数。另外推导出两种维生素的侧链几乎与磷脂的myristoyl链平行定向。

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    Univ Murcia Fac Vet Dept Bioquim &

    Biol Mol A Reg Campus Int Excellence Campus Mare Nostrum E-30080 Murcia Spain;

    Univ Murcia Fac Vet Dept Bioquim &

    Biol Mol A Reg Campus Int Excellence Campus Mare Nostrum E-30080 Murcia Spain;

    Univ Murcia Fac Vet Dept Bioquim &

    Biol Mol A Reg Campus Int Excellence Campus Mare Nostrum E-30080 Murcia Spain;

    Univ Murcia Fac Vet Dept Bioquim &

    Biol Mol A Reg Campus Int Excellence Campus Mare Nostrum E-30080 Murcia Spain;

    Univ Murcia Fac Vet Dept Bioquim &

    Biol Mol A Reg Campus Int Excellence Campus Mare Nostrum E-30080 Murcia Spain;

    Univ Murcia Fac Vet Dept Bioquim &

    Biol Mol A Reg Campus Int Excellence Campus Mare Nostrum E-30080 Murcia Spain;

    Univ Murcia Fac Vet Dept Bioquim &

    Biol Mol A Reg Campus Int Excellence Campus Mare Nostrum E-30080 Murcia Spain;

    Univ Murcia Fac Vet Dept Bioquim &

    Biol Mol A Reg Campus Int Excellence Campus Mare Nostrum E-30080 Murcia Spain;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 物理化学(理论化学)、化学物理学;化学;
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