MAGNETOFERRITIN - CHARACTERIZATION OF A NOVEL SUPERPARAMAGNETIC MR CONTRAST AGENT
MAGNETOFERRITIN - CHARACTERIZATION OF A NOVEL SUPERPARAMAGNETIC MR CONTRAST AGENT
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DOI:
10.1002/jmri.1880040343
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发表时间:
1994-05-01
影响因子:
4.4
通讯作者:
FRANK, JA
中科院分区:
文献类型:
--
作者:
BULTE, JWM;DOUGLAS, T;FRANK, JA
A protein-encaged superparamagnetic iron oxide has been developed and characterized hy using horse spleen apoferritin as a novel bioreactive environment. The roughly spherical magnetoferritin molecules, 120 angstrom in diameter, are composed of a monocrystalline maghemite or magnetite core 73 angstrom +/- 14 in diameter. Except for the additional presence of iron-rich molecules of higher molecular weight, the appearance and molecular weight (450 kd) of magnetoferritin are identical to that of natural ferritin; the molecules are externally indistinguishable from their precursor, with a pI (isoelectric point) in the range 4.3-4.6. The measured magnetic moment of the superparamagnetic cores is 13,200 Bohr magnetons per molecule, with TI and T2 relaxivities (r1 and r2) of 8 and 175 L.mmol-1 (Fe).sec-1, respectively, at body temperature and clinical field strengths. The unusually high r2/r1 ratio of 22 is thought to arise from ideal core composition, with no evidence of crystalline paramagnetic inclusions. T2 relaxation enhancement can be well correlated to the field-dependent molecular magnetization, as given by the Langevin magnetization function, raised to a power in the range 1.4-1.6. With its nanodimensional biomimetic protein cage as a rigid, convenient matrix for complexing a plethora of bioactive substances, magnetoferritin may provide a novel template for specific targeting of selected cellular sites.