研究者Kai Johnsson教授说道，我们给萤光素酶添加了一种小型化学标记，这种标记可以检测靶向蛋白，而荧光素酶则为我们提供了一种光信号来让我们用肉眼就可以识别；早在2014年研究者就开发出了一种快速简单的药物监测分子，而本文研究中，研究者标新立异，绕过蛋白质工程的麻烦，通过对荧光素酶突变来使其对靶向蛋白更加敏感，同时给荧光素酶吸附上了一种小分子标记。
这种标记可以作为一种开关，当其阻断荧光素酶表达时就会抑制发光，而当标记检测到靶向蛋白时，其就会停止对荧光素酶的阻断作用，从而荧光素酶就会发光，产生光信号来指示靶向蛋白的存在，简而言之，科学家们开发了一种针对生物学问题的化学溶液。Kai Johnsson指出，你可以想象一下被标记的荧光素酶作为机器分子，半生物半合成性的，那么你如何使得荧光素酶对突变蛋白的存在产生敏感性反应呢？这就需要大量的工作，而利用化学“技术”我们所要担心的就是设计一种合适的标记来识别靶向蛋白。
当检测到靶向蛋白存在时荧光素酶就会被激活发光，从而就可以使得肉眼足以看到，这就意味着这种特殊的系统并不会要求昂贵复杂的读出设备进行结果报告。最后研究者表示，这种新型技术具有非常广泛的用途，其是一种新时代的革新设计，该技术向我们展示的是我们如何利用合成化学技术来开发复杂的生物传感器蛋白。
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Modulating protein activity using tethered ligands with mutually exclusive binding sites
Alberto Schena, Rudolf Griss & Kai Johnsson
The possibility to design proteins whose activities can be switched on and off by unrelated effector molecules would enable applications in various research areas, ranging from biosensing to synthetic biology. We describe here a general method to modulate the activity of a protein in response to the concentration of a specific effector. The approach is based on synthetic ligands that possess two mutually exclusive binding sites, one for the protein of interest and one for the effector. Tethering such a ligand to the protein of interest results in an intramolecular ligand–protein interaction that can be disrupted through the presence of the effector. Specifically, we introduce a luciferase controlled by another protein, a human carbonic anhydrase whose activity can be controlled by proteins or small molecules in vitro and on living cells, and novel fluorescent and bioluminescent biosensors.