In Situ Ligation of High- and Low-Affinity Ligands to Cell Surface Receptors Enables Highly Selective Recognition.
In Situ Ligation of High- and Low-Affinity Ligands to Cell Surface Receptors Enables Highly Selective Recognition.
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DOI：
10.1002/advs.201700147
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发表时间：
2017-11
期刊：
影响因子：
--
通讯作者：
Tanaka K
中科院分区：
文献类型：
--
作者：
Taichi M;Nomura S;Nakase I;Imamaki R;Kizuka Y;Ota F;Dohmae N;Kitazume S;Taniguchi N;Tanaka K
本文报道了一个完全未被探索的概念，即通过在靶细胞表面原位连接高亲和力和低亲和力的配体来同时识别两个受体。这种从头开始的方法受到分子成像中经常应用的前靶向策略的启发，现在已经发展成为以高成像对比度可视化靶细胞的新范例的基础。使用标记的低亲和力配体(如葡聚糖)的一个明显优点是，可以将多余的标记配体从细胞中洗掉，而结合到细胞上的配体，即使在毫摩尔亲和力水平上，也可以通过与表面上预先定位的高亲和力配体进行生物正交反应来锚定。因此，非特定背景被最小化，从而提高了成像对比度。重要的是，尽管以前没有人探索过分子成像，但众所周知的是，糖/凝集素相互作用很弱，现在可以用作靶标的高度选择性配体。
This paper reports an entirely unexplored concept of simultaneously recognizing two receptors using high‐ and low‐affinity ligands through ligating them in situ on the target cell surface. This de novo approach is inspired by the pretargeting strategy frequently applied in molecular imaging, and has now evolved as the basis of a new paradigm for visualizing target cells with a high imaging contrast. A distinct advantage of using a labeled low‐affinity ligand such as glycan is that the excess labeled ligand can be washed away from the cells, whereas the ligand bound to the cell, even at the milli molar affinity level, can be anchored by a bioorthogonal reaction with a pretargeted high‐affinity ligand on the surface. Consequently, nonspecific background is minimized, leading to improved imaging contrast. Importantly, despite previously unexplored for molecular imaging, a notoriously weak glycan/lectin interaction can now be utilized as a highly selective ligand to the targets.
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