110990-09-5Relevant articles and documents
Identification of Annexin A2 as a target protein for plant alkaloid matrine
Wang, Dongyao,Cao, Yan,Zheng, Leyi,Lv, Diya,Chen, Langdong,Xing, Xinrui,Zhu, Zhenyu,Li, Xiaoyu,Chai, Yifeng
, p. 5020 - 5023 (2017)
Matrine is a plant alkaloid and a major active component in the Chinese medical herb Sophora flavescens. Matrine has shown potent anti-cancer activities but its molecular target(s) and mechanism are still unknown. Using the photo-affinity labeling approach, for the first time, Annexin A2 was identified as a direct-binding target of matrine in cancer cells.
Target Identification of Kinase Inhibitor Alisertib (MLN8237) by Using DNA-Programmed Affinity Labeling
Wang, Dong-Yao,Cao, Yan,Zheng, Le-Yi,Chen, Lang-Dong,Chen, Xiao-Fei,Hong, Zhan-Ying,Zhu, Zhen-Yu,Li, Xiaoyu,Chai, Yi-Feng
, p. 10906 - 10914 (2017)
Accurate identification of the molecular targets of bioactive small molecules is a highly important yet challenging task in biomedical research. Previously, a method named DPAL (DNA-programmed affinity labeling) for labeling and identifying the cellular targets of small molecules and nucleic acids was developed. Herein, DPAL is applied for the target identification of Alisertib (MLN8237), which is a highly specific aurora kinase A (AKA) inhibitor and a drug candidate being tested in clinical trials for cancer treatment. Apart from the well-established target of AKA, several potential new targets of MLN8237 were identified. Among them, p38 mitogen-activated protein kinase (p38) and laminin receptor (LAMR) were validated to be implicated in the anticancer activities of MLN8237. Interestingly, these new targets were not identified with non-DNA-based affinity probes. This work may facilitate an understanding of the molecular basis of the efficacy and side effects of MLN8237 as a clinical drug candidate. On the other hand, this work has also demonstrated that the method of DPAL could be a useful tool for target identification of bioactive small molecules.
Activity-based high-throughput profiling of metalloprotease inhibitors using small molecule microarrays
Wang, Jun,Uttamchandani, Mahesh,Li, Ping Sun,Yao, Shao Q.
, p. 717 - 719 (2008/02/03)
We herein describe a high-throughput small molecule microarray (SMM) method that enables quick and cost-effective identification of potent inhibitors of metalloproteases in an activity-dependent manner, thereby offering a rapid means for inhibitor discove
