Flood Ronan J, Ramberg Kiefer O, Mengel Darius B, Guagnini Francesca, Crowley Peter B
SSPC, Science Foundation Ireland Research Centre for Pharmaceuticals, School of Biological and Chemical Sciences, National University of Ireland Galway, University Road, Galway H91 TK33, Ireland.
Cryst Growth Des. 2022 May 4;22(5):3271-3276. doi: 10.1021/acs.cgd.2c00108. Epub 2022 Feb 22.
Controlled protein assembly provides a means to generate biomaterials. Synthetic macrocycles such as the water-soluble sulfonato-calix[n]arenes are useful mediators of protein assembly. Sulfonato-thiacalix[4]arene ( ), with its metal-binding capacity, affords the potential for simultaneous macrocycle- and metal-mediated protein assembly. Here, we describe the -/Zn-directed assembly of two proteins: cationic α-helical cytochrome (cyt ) and neutral β-propeller lectin (RSL). Two co-crystal forms were obtained with cyt , each involving multinuclear zinc sites supported by the cone conformation of . The /Zn cluster acted as an assembly node via both lysine encapsulation and metal-mediated protein-protein contacts. In the case of RSL, adopted the 1,2-alternate conformation and supported a dinuclear zinc site with concomitant encapsulation and metal-binding of two histidine side chains. These results, together with the knowledge of thiacalixarene/metal nanoclusters, suggest promising applications for thiacalixarenes in biomaterials and MOF fabrication.
可控蛋白质组装提供了一种生成生物材料的方法。合成大环化合物，如水溶性磺化杯[n]芳烃，是蛋白质组装的有用介质。具有金属结合能力的磺化硫代杯[4]芳烃能够实现大环和金属介导的蛋白质同时组装。在此，我们描述了由磺化硫代杯[4]芳烃/锌导向的两种蛋白质的组装：阳离子α-螺旋细胞色素c（cyt c）和中性β-螺旋桨豆凝集素（RSL）。与细胞色素c一起获得了两种共晶形式，每种形式都涉及由磺化硫代杯[4]芳烃的锥式构象支撑的多核锌位点。磺化硫代杯[4]芳烃/锌簇通过赖氨酸包封和金属介导的蛋白质-蛋白质接触充当组装节点。在RSL的情况下，磺化硫代杯[4]芳烃采取1,2-交替构象并支撑一个双核锌位点，同时包封和结合两个组氨酸侧链。这些结果，连同对硫代杯芳烃/金属纳米簇的了解，表明硫代杯芳烃在生物材料和金属有机框架制造方面具有广阔的应用前景。
