The Bacterial Hydrophobin BslA is a Switchable Ellipsoidal Janus Nanocolloid

The Bacterial Hydrophobin BslA is a Switchable Ellipsoidal Janus Nanocolloid
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DOI:
10.1021/acs.langmuir.5b02347
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发表时间:
2015-10-27
期刊:
影响因子:
3.9
通讯作者:
Zachariae, Ulrich
Zachariae, Ulrich
中科院分区:
化学2区
文献类型:
--
作者:
Brandani, Giovanni B.;Schor, Marieke;Zachariae, Ulrich

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BslA是一种两亲性蛋白,在枯草芽孢杆菌生物膜周围形成高度疏水的外壳,保护细菌群落不受外界水溶液的影响。它具有独特的结构,在亲水性和疏水性表面之间具有明显的分区。这种表面性质使人联想到合成的Janus胶体。通过一组基于实验数据的多尺度模拟来研究BslA变体在水-环己烷界面上的行为,我们表明BslA确实代表了椭球Janus纳米粒子的生物学例子,而且其表面相互作用是容易切换的。BslA包含一个局部构象开关,控制其对水-油界面的整体亲和力和取向。这种适应性与单点突变一起,使其溶剂和界面相互作用得以微调,并表明BsIA可能成为生物技术应用的基础。
BslA is an amphiphilic protein that forms a highly hydrophobic coat around Bacillus subtilis biofilms, shielding the bacterial community from external aqueous solution. It has a unique structure featuring a distinct partition between hydrophilic and hydrophobic surfaces. This surface property is reminiscent of synthesized Janus colloids. By investigating the behavior of BslA variants at water-cyclohexane interfaces through a set of multiscale simulations informed by experimental data, we show that BslA indeed represents a biological example of an ellipsoidal Janus nanoparticle, whose surface interactions are, moreover, readily switchable. BslA contains a local conformational toggle, which controls its global affinity for, and orientation at, water oil interfaces. This adaptability, together with single-point mutations, enables the fine-tuning of its solvent and interfacial interactions, and suggests that BsIA could be a basis for biotechnological applications.