Department of Mechanical Engineering, Korea University, 02841, Seoul, Republic of Korea.
Department of Mechanical Engineering, Korea University, 02841, Seoul, Republic of Korea.
Colloids Surf B Biointerfaces. 2020 Nov;195:111269. doi: 10.1016/j.colsurfb.2020.111269. Epub 2020 Jul 26.
Hydrophobins are fungal proteins that can mediate water surface tension by forming amphiphilic self-assembly structures in hydrophobic-hydrophilic interfaces. Hydrophobins are known to self-assemble into two forms depending on their class: class I hydrophobins aggregate into a functional amyloid rodlet, while class II hydrophobins aggregate into a regularly patterned monolayer. Owing to its unique properties, hydrophobin has been considered as a biocompatible nanomaterial for various applications and there have been several attempts to engineer hydrophobins to enhance their function. Recently, a chimeric hydrophobin named NChi2 was found to be able to self-assemble into both rodlet and monolayer forms depending on the incubating environment. Although this remarkable feature suggests that NChi2 can function as a versatile bionanomaterial for various applications, only little information about the protein, such as its assembly structure or its characteristics, is provided. To investigate the extraordinary behavior of NChi2, it seems to be a prerequisite to first understand the characteristics of its parent hydrophobins, namely class I EAS and class II NC2. Here, we conducted a preliminary study on predicting the self-assembly structure of class II hydrophobin NC2 and estimating its structural characteristics by employing several computational methods. From the results, we found that NC2 shows stronger surface activity than HFBII, while its assembly structure is weaker than that of HFBII. We hope that this research serves as a foundation to further investigate the structural characteristics of a unique hydrophobin NChi2 in future studies.
水蛋白是一种真菌蛋白，能够在疏水性-亲水性界面形成两亲自组装结构，从而介导水表面张力。根据其类别，水蛋白已知可自组装成两种形式：I 类水蛋白聚集成功能性淀粉样纤维束，而 II 类水蛋白聚集成规则图案的单层。由于其独特的性质，水蛋白已被认为是一种适用于各种应用的生物相容纳米材料，并且已经有几种尝试对水蛋白进行工程改造以增强其功能。最近，发现一种名为 NChi2 的嵌合水蛋白能够根据孵育环境自组装成纤维束和单层两种形式。尽管这种显著的特性表明 NChi2 可以作为一种多功能的生物纳米材料应用于各种应用，但关于该蛋白质的信息，例如其组装结构或特性，仅提供了很少的信息。为了研究 NChi2 的非凡行为，似乎首先需要了解其亲本水蛋白（即 I 类 EAS 和 II 类 NC2）的特性。在这里，我们通过使用几种计算方法对 II 类水蛋白 NC2 的自组装结构进行了初步预测，并对其结构特性进行了估算。结果表明，NC2 比 HFBII 具有更强的表面活性，但其组装结构比 HFBII 弱。我们希望这项研究能够为进一步研究独特水蛋白 NChi2 的结构特性提供基础，以在未来的研究中进行研究。
