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Hydropathy: the controlling factor behind the inhibition of Aβ fibrillation by graphene oxide

机译:水疗法:石墨烯氧化物抑制β纤维化的控制因子

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Protein and peptide aggregation/fibrillation is reported to be responsible for several neurological disorders. Fibrillation of the amyloid β-peptide fragment (25–35) which is a biologically active region of the full length peptide, has been observed to be significantly inhibited in presence of the two dimensional nanomaterial graphene oxide (GO). Fibrillation and inhibition of the Aβ _(25–35) peptide by GO has been performed at 37 °C at physiological pH (pH 7.4). The inhibition process is monitored by ThioflavinT fluorescence (ThT), circular dichroism spectroscopy, matrix assisted laser desorption/ionization mass spectrometry, dynamic light scattering experiments etc. The soluble fraction of the protein is quantified by the BCA assay. Microscopic techniques are used to study the morphology of the fibrils formed. GO is observed to inhibit the fibrillation even at very low concentrations and is amplified with increase in concentration of GO. ThT kinetic data fitted well with a sigmoidal curve and shows that GO is able to lengthen the lag phase of the fibrillation process. It appears that surface adsorption of protein on the nanomaterial prevents the monomers to come together. It is speculated that the presence of both polar and non-polar moieties in GO interact strongly with the hydrophobic and hydrophilic residues of the Aβ _(25–35) peptide monomer units, thus preventing further aggregation.
机译:据报道,蛋白质和肽聚集/纤维化是对几种神经疾病的原因。已经观察到是全长肽的生物活性区域的淀粉样蛋白β-肽片段(25-35)的原纤化,以在二维纳米材料石墨烯(GO)的存在下显着抑制。通过GO在生理pH(pH7.4)下在37℃下在37℃下进行Aβ_(25-35)肽的原纤化和抑制。通过硫酰伐荧光(THT),圆形二色光谱,基质辅助激光解吸/电离质谱,动态光散射实验等监测抑制作用。蛋白质的可溶部分通过BCA测定量化。微观技术用于研究形成的原纤维的形态。即使在非常低的浓度下,观察到抑制原纤化,并且随着GO浓度的增加而扩增。动力学数据与丝状曲线合理,并表明可以延长原纤化过程的滞后阶段。似乎蛋白质在纳米材料上吸附的表面吸附可防止单体聚集在一起。推测,在Aβ_(25-35)肽单体单元的疏水性和亲水残留的情况下,POL极性和非极性部分的存在强烈地相互作用,从而防止进一步的聚集。

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