背景(考古学)
纳米技术
配体(生物化学)
机制(生物学)
材料科学
工作(物理)
生物物理学
化学
物理
生物
受体
生物化学
量子力学
热力学
古生物学
作者
Rongying Liu,Long Li,Shuyu Chen,Zhiwei Yang,Zdravko Kochovski,Shilin Mei,Yan Lü,Lei Zhang,Guosong Chen
出处
期刊:ACS Nano
[American Chemical Society]
日期:2023-01-17
卷期号:17 (3): 2245-2256
被引量:3
标识
DOI:10.1021/acsnano.2c08583
摘要
A protein assembly with the ability to switch interplay modes of multiple driving forces has been achieved. Although biomolecular systems driven by multiple driving forces have been exploited, work on such a protein assembly capable of switching the interplay modes at nanoscale has been rarely reported so far as a result of their great fabrication challenge. In this work, two sets of driving forces such as ligand-ligand interaction and protein-protein interaction were leveraged to antagonistically underpin the multilayered stackings and trigger the hollow evolution to afford the well-defined hollow rectangular frame of proteins. While these protein frames further collapsed into aggregates, the ligand-ligand interactions were weakened, and the interplay of two sets of driving forces thereby tended to switch into synergistic mode, converting the protein packing mode from porously loose packing to axially dense packing and thus giving rise to a morphological evolution toward a nanosized protein tube. This strategy not only provides a nanoscale understanding on the mechanism underlying the switch of interplay modes in the context of biomacromolecules but also may provide access for diverse sophisticated biomacromolecular nanostructures that are historically inaccessible for conventional self-assembly strategies.
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