Choi Hyeongjoo, Jung Yongwon
Department of Chemistry, KAIST 291 Daehak-ro, Yuseong-gu Daejeon 34143 Republic of Korea
Chem Sci. 2022 Jun 8;13(25):7552-7559. doi: 10.1039/d1sc06993d. eCollection 2022 Jun 29.
Precise control of the number of conjugated proteins on a nanoparticle surface has long been a highly challenging task. Here, we developed a one-pot, purification-free strategy for valency-controlled conjugation of tandem repeat protein chains on gold nanoparticles. Protein chains were designed to contain multiple, regularly spaced binding modules, which can multivalently interact with coating molecules on nanoparticle surfaces. We discovered that a slow increase of this interaction strength facilitates full participation of repeated binding modules on a protein chain for surface binding (as well as dynamic rearrangement) on a single nanoparticle, which resulted in stable protein chain wrapping around nanoparticles. By varying the protein chain length, a defined number of protein chains were conjugated on gold nanoparticles with difference sizes. Various high-order nanoparticle structures were accurately assembled with these valence-controlled protein-particle conjugates. The present strategy offers a highly dynamic but controlled protein coating approach on solid surfaces of diverse nanostructures. In addition, this work also provides a valuable clue to understand dynamic binding processes of multivalent repeat proteins.
长期以来，精确控制纳米颗粒表面共轭蛋白的数量一直是一项极具挑战性的任务。在此，我们开发了一种无需纯化的一锅法策略，用于在金纳米颗粒上进行价态控制的串联重复蛋白链共轭。设计的蛋白链包含多个规则间隔的结合模块，这些模块可以与纳米颗粒表面的包被分子进行多价相互作用。我们发现，这种相互作用强度的缓慢增加有助于蛋白链上重复结合模块充分参与单个纳米颗粒表面的结合（以及动态重排），从而导致蛋白链稳定地包裹在纳米颗粒周围。通过改变蛋白链长度，在不同尺寸的金纳米颗粒上共轭了确定数量的蛋白链。利用这些价态控制的蛋白-颗粒共轭物精确组装了各种高阶纳米颗粒结构。本策略为在各种纳米结构的固体表面提供了一种高度动态但可控的蛋白包被方法。此外，这项工作还为理解多价重复蛋白的动态结合过程提供了有价值的线索。
