Mejias Sara H, Couleaud Pierre, Casado Santiago, Granados Daniel, Garcia Miguel Angel, Abad Jose M, Cortajarena Aitziber L
IMDEA-Nanociencia and Centro Nacional de Biotecnología (CNB-CSIC)-IMDEA Nanociencia Associated Unit, Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain.
Instituto de Cerámica y Vidrio (ICV-CSIC), Cantoblanco, 28049 Madrid, Spain; Instituto de Magnetismo Aplicado "Salvador Velayos", UCM-ADIF, 28230 Madrid, Spain.
Colloids Surf B Biointerfaces. 2016 May 1;141:93-101. doi: 10.1016/j.colsurfb.2016.01.039. Epub 2016 Jan 22.
The controlled assembly of building blocks to achieve new nanostructured materials with defined properties at different length scales through rational design is the basis and future of bottom-up nanofabrication. This work describes the assembly of the idealized protein building block, the consensus tetratricopeptide repeat (CTPR), into monolayers by oriented immobilization of the blocks. The selectivity of thiol-gold interaction for an oriented immobilization has been verified by comparing a non-thiolated protein building block. The physical properties of the CTPR protein thin biomolecular films including topography, thickness, and viscoelasticity, are characterized. Finally, the ability of these scaffolds to act as templates for inorganic nanostructures has been demonstrated by the formation of well-packed gold nanoparticles (GNPs) monolayer patterned by the CTPR monolayer.
通过合理设计，将构建模块进行可控组装以在不同长度尺度上获得具有特定性质的新型纳米结构材料，是自下而上纳米制造的基础和未来发展方向。这项工作描述了通过对理想蛋白质构建模块——共有四肽重复序列（CTPR）进行定向固定，使其组装成单分子层。通过比较未硫醇化的蛋白质构建模块，验证了硫醇-金相互作用对定向固定的选择性。对CTPR蛋白质薄生物分子膜的物理性质进行了表征，包括形貌、厚度和粘弹性。最后，通过由CTPR单分子层图案化形成排列紧密的金纳米颗粒（GNP）单分子层，证明了这些支架作为无机纳米结构模板的能力。
