Zhu Biyue, Yang Jing, Van Richard, Yang Fan, Yu Yue, Yu Astra, Ran Kathleen, Yin Keyi, Liang Yingxia, Shen Xunuo, Yin Wei, Choi Se Hoon, Lu Ying, Wang Changning, Shao Yihan, Shi Liang, Tanzi Rudolph E, Zhang Can, Cheng Yan, Zhang Zhirong, Ran Chongzhao
Athinoula A. Martinos Center for Biomedical Imaging, Department of Radiology, Massachusetts General Hospital/Harvard Medical School Charlestown Boston Massachusetts USA 02129
Key Laboratory of Drug Targeting and Drug Delivery Systems, West China School of Pharmacy, Sichuan University Chengdu 610041 China
Chem Sci. 2022 Jun 28;13(27):8104-8116. doi: 10.1039/d2sc02819k. eCollection 2022 Jul 13.
Small molecules and antibodies are normally considered separately in drug discovery, except in the case of covalent conjugates. We unexpectedly discovered several small molecules that could inhibit or enhance antibody-epitope interactions which opens new possibilities in drug discovery and therapeutic modulation of auto-antibodies. We first discovered a small molecule, CRANAD-17, that enhanced the binding of an antibody to amyloid beta (Aβ), one of the major hallmarks of Alzheimer's disease, by stable triplex formation. Next, we found several small molecules that altered antibody-epitope interactions of tau and PD-L1 proteins, demonstrating the generality of this phenomenon. We report a new screening technology for ligand discovery, screening platform based on epitope alteration for drug discovery (SPEED), which is label-free for both the antibody and small molecule. SPEED, applied to an Aβ antibody, led to the discovery of a small molecule, GNF5837, that inhibits Aβ aggregation and another, obatoclax, that binds Aβ plaques and can serve as a fluorescent reporter in brain slices of AD mice. We also found a small molecule that altered the binding between Aβ and auto-antibodies from AD patient serum. SPEED reveals the sensitivity of antibody-epitope interactions to perturbation by small molecules and will have multiple applications in biotechnology and drug discovery.
在药物研发中,小分子和抗体通常是分开考虑的,共价偶联物的情况除外。我们意外地发现了几种能够抑制或增强抗体-表位相互作用的小分子,这为药物研发和自身抗体的治疗调节开辟了新的可能性。我们首先发现了一种小分子CRANAD-17,它通过稳定的三链体形成增强了抗体与淀粉样β蛋白(Aβ)的结合,Aβ是阿尔茨海默病的主要标志之一。接下来,我们发现了几种小分子改变了tau蛋白和PD-L1蛋白的抗体-表位相互作用,证明了这种现象的普遍性。我们报告了一种用于配体发现的新筛选技术,即基于表位改变的药物发现筛选平台(SPEED),该平台对抗体和小分子均无需标记。将SPEED应用于一种Aβ抗体,发现了一种小分子GNF5837,它能抑制Aβ聚集,另一种小分子obatoclax能结合Aβ斑块,可作为AD小鼠脑切片中的荧光报告分子。我们还发现了一种小分子改变了Aβ与AD患者血清中自身抗体之间的结合。SPEED揭示了抗体-表位相互作用对小分子干扰的敏感性,并将在生物技术和药物发现中有多种应用。