Lipid cubic phases as stable nanochannel network structures for protein biochip development: X-ray diffraction study

Lipid cubic phases as stable nanochannel network structures for protein biochip development: X-ray diffraction study
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DOI:
10.1021/la0345284
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发表时间:
2003-08-19
期刊:
影响因子:
3.9
通讯作者:
Bourgaux, C
Bourgaux, C
中科院分区:
化学2区
文献类型:
--
作者:
Angelova, A;Ollivon, M;Bourgaux, C

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生物相容的纳米通道和三维(3D)周期性的介孔结构促进了蛋白质在天然构象中的包埋,构成了蛋白质生物芯片和亲和生物传感器等快速发展领域感兴趣的有组织的保护介质。在生理水化条件下,在非片层脂类单油酸酯(MO)和马来酰亚胺(三甘醇)醚脂(MTEG)的自组装混合物中形成了具有反应性化学基团的三维周期性纳米通道结构,并用高分辨率的时间分辨同步X射线衍射仪在3-96℃的温度范围内对其进行了研究。监测了空间群Pn3m和Im3m的两个非片层立方相Q(224)和Q(229)的形成机制和结构参数。以MO/MTEG为基础的免疫胶体和蛋白胶体混合物在高浓度下与免疫球蛋白Fab片段、完整的免疫球蛋白、白蛋白、转铁蛋白和纤维蛋白原孵育后的结构相行为表明,立方晶格在过量的水中以纳米结构的通道网络存在。对于感兴趣的特定脂类组成,蛋白质类型只能微调这些通道网络,它们似乎在较宽的温度区间内保持稳定。提出了一种三维立方体脂质网络中蛋白质包埋的新机制。
Biocompatible nanochannel and mesoporous structures of a three-dimensional (3D) periodicity, facilitating protein entrapment at native conformations, constitute organized protective media of interest for the fast developing fields of protein biochips and affinity biosensors. Three-dimensional periodic nanochannel structures possessing reactive chemical groups, surface-exposed to the aqueous phase, are formed here in self-assembled mixtures of a nonlamellar lipid glycerylmonooleate (MO) and a maleimide(triethylene glycol)ether lipid (MTEG) under physiological hydration conditions and are investigated by high-resolution time-resolved synchrotron X-ray diffraction in the interval from 3 to 96 degreesC. The mechanism of formation and the structural parameters of two nonlamellar cubic phases Q(224) and Q(229) (of space groups Pn3m and Im3m) are monitored. The structural phase behavior of the MO/MTEG-based immunocubosome and proteocubosome mixtures, obtained upon incubation with immunoglobulin Fab fragments, whole IgG, albumin, transferrin, and fibrinogen at high concentrations, indicates that the cubic lattices exist in excess water as nanostructured channel networks. With the particular lipid composition of interest, the protein type only finely tunes these channel networks and they appear to be stable over a broad temperature interval. A new mechanism of protein entrapment within the 3D cubosome lipid networks is proposed.