Department of Chemistry, Korea University, Seoul, 02841, Republic of Korea.
Department of Chemistry, Pohang University of Science and Technology (POSTECH), Pohang, 37673, Republic of Korea.
Sci Rep. 2017 Jul 18;7(1):5710. doi: 10.1038/s41598-017-06181-4.
Amyloid fibrils have recently been highlighted for their diverse applications as functional nanomaterials in modern chemistry. However, tight control to obtain a targeted fibril length with low heterogeneity has not been achieved because of the complicated nature of amyloid fibrillation. Herein, we demonstrate that fibril assemblies can be homogeneously manipulated with desired lengths from ~40 nm to ~10 μm by a phase transfer of amyloid proteins based on host-guest chemistry. We suggest that host-guest interactions with cucurbit[6]uril induce a phase transfer of amyloid proteins (human insulin, human islet amyloid polypeptide, hen egg lysozyme, and amyloid-β 1-40 & 1-42) from the soluble state to insoluble state when the amount of cucurbit[6]uril exceeds its solubility limit in solution. The phase transfer of the proteins kinetically delays the nucleation of amyloid proteins, while the nuclei formed in the early stage are homogeneously assembled to fibrils. Consequently, supramolecular assemblies of amyloid proteins with heterogeneous kinetics can be controlled by protein phase transfer based on host-guest interactions.
淀粉样纤维最近因其作为现代化学中功能性纳米材料的多种应用而受到关注。然而，由于淀粉样纤维形成的复杂性，要获得具有低异质性的目标纤维长度的严格控制尚未实现。在此，我们证明了基于主客体化学的淀粉样蛋白的相转移可以均匀地操纵纤维组装体，使其具有所需的长度，从40nm 到10μm。我们提出，当葫芦[6]脲的量超过其在溶液中的溶解度极限时，主客体相互作用会诱导淀粉样蛋白（人胰岛素、人胰岛淀粉样多肽、鸡卵溶菌酶和淀粉样-β1-40 和 1-42）从可溶状态到不溶状态的相转移。蛋白质的相转移在动力学上延迟了淀粉样蛋白的成核，而在早期形成的核则均匀地组装成纤维。因此，基于主客体相互作用的蛋白质相转移可以控制具有不同动力学的淀粉样蛋白的超分子组装。
