Characterizing and Controlling Nanoscale Self-Assembly of Suckerin-12,ACS Synthetic Biology

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Characterizing and Controlling Nanoscale Self-Assembly of Suckerin-12
ACS Synthetic Biology ( IF 3.7 ) Pub Date : 2020-11-17 , DOI: 10.1021/acssynbio.0c00442
Jasmine M. Hershewe _{1,

2,

3} , William D. Wiseman _{2,

3,

4} , James E. Kath _{1,

2,

3} , Chelsea C. Buck _{5,

6} , Maneesh K. Gupta ₅ , Patrick B. Dennis ₅ , Rajesh R. Naik ₇ , Michael C. Jewett _{1,

2,

3,

8,

9}

Affiliation

Department of Chemical and Biological Engineering, Northwestern University, 2145 Sheridan Road, Technological Institute E136, Evanston, Illinois 60208−3120, United States
Chemistry of Life Processes Institute, Northwestern University, 2170 Campus Drive, Evanston, Illinois 60208−3120, United States
Center for Synthetic Biology, Northwestern University, 2145 Sheridan Road, Technological Institute E136, Evanston, Illinois 60208−3120, United States
Master of Biotechnology Program, Technological Institute, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208−3120, United States
Materials and Manufacturing Directorate, Air Force Research Laboratory, Wright-Patterson Air Force Base, Dayton, Ohio 45433, United States
Chemical and Materials Engineering Department, University of Dayton, 300 College Park Avenue, Dayton, Ohio 45469, United States
711th Human Performance Wing, Air Force Research Laboratory, Wright-Patterson Air Force Base, Dayton, Ohio 45433, United States
Robert H. Lurie Comprehensive Cancer Center, Northwestern University, 676 North Saint Clair Street, Suite 1200, Chicago, Illinois 60611−3068, United States
Simpson Querrey Institute, Northwestern University, 303 East Superior Street, Suite 11-131, Chicago, Illinois 60611−2875, United States

Structural proteins such as “suckerins” present promising avenues for fabricating functional materials. Suckerins are a family of naturally occurring block copolymer-type proteins that comprise the sucker ring teeth of cephalopods and are known to self-assemble into supramolecular networks of nanoconfined β-sheets. Here, we report the characterization and controllable, nanoscale self-assembly of suckerin-12 (S12). We characterize the impacts of salt, pH, and protein concentration on S12 solubility, secondary structure, and self-assembly. In doing so, we identify conditions for fabricating ∼100 nm nanoassemblies (NAs) with narrow size distributions. Finally, by installing a noncanonical amino acid (ncAA) into S12, we demonstrate the assembly of NAs that are covalently conjugated with a hydrophobic fluorophore and the ability to change self-assembly and β-sheet content by PEGylation. This work presents new insights into the biochemistry of suckerin-12 and demonstrates how ncAAs can be used to expedite and fine-tune the design of protein materials.

中文翻译：

表征和控制Suckerin-12的纳米级自组装。

结构蛋白（例如“ suckerins”）为制造功能材料提供了有希望的途径。Suckerins是一类天然存在的嵌段共聚物型蛋白质，包含头足类动物的吸盘环齿，并且已知能够自组装成纳米级β-折叠的超分子网络。在这里，我们报告suckerin-12（S12）的表征和可控的纳米级自组装。我们表征了盐，pH和蛋白质浓度对S12溶解度，二级结构和自组装的影响。通过这样做，我们确定了制造窄尺寸分布的〜100 nm纳米组件（NA）的条件。最后，通过在S12中安装非规范氨基酸（ncAA），我们证明了与疏水性荧光团共价结合的NAs的组装以及通过聚乙二醇化改变自组装和β-折叠含量的能力。这项工作提出了关于suckerin-12的生物化学的新见解，并展示了如何使用ncAA来加速和微调蛋白质材料的设计。

更新日期：2020-12-18

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