在自然界中，生物體內具有許多高度有序的結構，生物分子可以透過自發性地從無序狀態自組裝成有序結構。近年來，許多研究人員對於分子自組裝產生極大的興趣。因此，我們使用奈米粒子排列形成最密堆積，奈米流體於粒子空隙用來引導蛋白質自組裝。我們使用原子力顯微鏡 (atomic force microscopy, AFM)來分析由不同奈米流體引導的蛋白質組裝陣列。由結果表明具有不同表面特性的奈米球模板會影響奈米顆粒表面與蛋白質之間的相互作用以及蛋白質組裝。由膠體或二氧化矽奈米球模板形成的兩種納米流體系統顯示出不同的蛋白質組裝機制。相對疏水的膠體模板通過蒸發和毛細管力引導蛋白質排列，而親水的二氧化矽奈米球模板會傾向形成蛋白質冠(protein corona)，蛋白質會在蒸發和組裝過程中吸附於二氧化矽奈米粒子的表面。此外，我們藉由控制濃度、奈米粒子的直徑、奈米粒子與蛋白質的比例，以製造具有不同形態的各種蛋白質組裝體陣列，例如同心環和週期性奈米纖維結構。在未來，我們希望利用這些蛋白質組裝陣列作為生物界面，模擬生物體內的特殊結構，並應用於生物醫學上。

In nature, the living organisms have many highly ordered structures. Biomolecules can spontaneously form ordered structures from disordered states through self-assembly. In recent years, many researchers have interests in molecular self-assembly. Hence, we used the nanoparticles that form the close-packed arrangement containing interstitial spaces to produce nanofluids for guiding proteins self-assembly. We used atomic force microscopy (AFM) to analyze the arrays of protein assemblies guided by different nanofluids. The results demonstrate that the colloidal templates with different surface properties would affect the interaction between the nanoparticle surface and the proteins as well as protein assembly. Two nanofluid systems formed with latex or silica colloidal templates show distinct mechanisms to assemble proteins. Relatively hydrophobic latex colloidal templates guide the proteins to arrange by evaporation and capillary forces while the hydrophilic silica colloidal templates prefer forming protein corona that the proteins would absorb on the surfaces of silica nanoparticles during evaporation and assembly process. Additionally, we controlled the concentrations, the diameters of nanoparticles, the volume ratio of nanoparticle-to-protein to fabricate various arrays of protein assemblies with different morphologies, such as concentric rings, and circular nanofibril. In the future, we would like to use those arrays of protein assemblies as biointerrfaces to imitate the special structures inside the living organism for biomedical applications.

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