Department of Chemistry, Technical University of Munich, Lichtenbergstrasse 4, 85748 Garching, Germany.
Department of Physics, Technical University of Munich, Am Coulombwall 4a, 85748 Garching, Germany.
J Am Chem Soc. 2020 Dec 9;142(49):20837-20844. doi: 10.1021/jacs.0c10486. Epub 2020 Nov 25.
In biology, self-assembly of proteins and energy-consuming reaction cycles are intricately coupled. For example, tubulin is activated and deactivated for assembly by a guanosine triphosphate (GTP)-driven reaction cycle, and the emerging microtubules catalyze this reaction cycle by changing the microenvironment of the activated tubulin. Recently, synthetic analogs of chemically fueled assemblies have emerged, but examples in which assembly and reaction cycles are reciprocally coupled remain rare. In this work, we report a peptide that can be activated and deactivated for self-assembly. The emerging assemblies change the microenvironment of their building blocks, which consequently accelerate the rates of building block deactivation and reactivation. We quantitatively understand the mechanisms at play, and we are thus able to tune the catalysis by molecular design of the peptide precursor.
在生物学中，蛋白质的自组装和耗能反应循环是紧密耦合的。例如，微管蛋白通过鸟苷三磷酸（GTP）驱动的反应循环被激活和失活，而新兴的微管则通过改变激活的微管蛋白的微环境来催化这个反应循环。最近，出现了化学燃料组装的合成类似物，但组装和反应循环相互耦合的例子仍然很少。在这项工作中，我们报告了一种可以被激活和失活以进行自组装的肽。新兴的组装体改变了它们构建块的微环境，这反过来又加速了构建块失活和再激活的速度。我们定量地理解了起作用的机制，因此能够通过肽前体的分子设计来调节催化作用。
