Biological Physics Department, University of Mons-Hainaut, Belgium.
Wiley Interdiscip Rev Nanomed Nanobiotechnol. 2009 May-Jun;1(3):299-310. doi: 10.1002/wnan.36.
Nanometric crystals of maghemite are known to exhibit superparamagnetism. Because of the significance of their magnetic moment, maghemite nanoparticles are exceptional contrast agents and are used for magnetic resonance imaging (of the liver, spleen, lymph nodes), for magnetic resonance angiography and for molecular and cellular imaging. The relaxivity of these agents depends on their size, saturation magnetization and magnetic field and also on their degree of clustering. There are different types of maghemite particles whose relaxation characteristics are suited to a specific MRI application. The relaxation induced by maghemite particles is caused by the diffusion of water protons in the inhomogeneous field surrounding the particles. This is well described by a theoretical model that takes magnetite crystal anisotropy and Néel relaxation into account. Another type of superparamagnetic compound is ferritin, the iron-storing protein: it contains a superparamagnetic ferrihydrite core. Even if the resulting magnetic moment of ferritin is far smaller than for magnetite nanoparticles, its massive presence in different organs darkens T(2)-weighted MR images, allowing the noninvasive estimation of iron content, thanks to MRI. The relaxation induced by ferritin in aqueous solutions has been demonstrated to be caused by the exchange of protons between bulk water protons and the surface of the ferrihydrite crystal. However, in vivo, the relaxation properties of ferritin are still unexplained, probably because of protein clustering.
已知磁赤铁矿的纳米晶体具有超顺磁性。由于其磁矩的重要性,磁赤铁矿纳米颗粒是特殊的对比剂,用于磁共振成像(肝脏、脾脏、淋巴结)、磁共振血管造影以及分子和细胞成像。这些造影剂的弛豫率取决于其尺寸、饱和磁化强度和磁场,以及其团聚程度。有不同类型的磁赤铁矿颗粒,其弛豫特性适合特定的 MRI 应用。磁赤铁矿颗粒引起的弛豫是由水质子在颗粒周围不均匀场中的扩散引起的。这可以通过考虑磁铁矿晶体各向异性和奈尔弛豫的理论模型来很好地描述。另一种超顺磁化合物是铁蛋白,即储铁蛋白:它含有超顺磁的水铁矿核。即使铁蛋白的磁矩远小于磁铁矿纳米颗粒,由于 MRI,其在不同器官中的大量存在会使 T2 加权 MR 图像变暗,从而可以非侵入性地估计铁含量。已经证明,在水溶液中,铁蛋白引起的弛豫是由体相水分子质子与水铁矿晶体表面之间的质子交换引起的。然而,在体内,铁蛋白的弛豫特性仍未得到解释,可能是由于蛋白质团聚。