https://www.selleckchem.com/products/s-2-hydroxysuccinic-acid.html Understanding the selectivity of methyltransferase inhibitors is important to dissecting the functions of each methyltransferase target. From this perspective, we report a chemoproteomic study to profile the selectivity of a potent protein N-terminal methyltransferase 1 (NTMT1) bisubstrate inhibitor NAH-C3-GPKK (Ki, app = 7 ± 1 nM) in endogenous proteomes. First, we describe the rational design, synthesis, and biochemical characterization of a new chemical probe 6, a biotinylated analogue of NAH-C3-GPKK. Next, we systematically analyze protein networks that may selectively interact with the biotinylated probe 6 in concert with the competitor NAH-C3-GPKK. Besides NTMT1, the designated NTMT1 bisubstrate inhibitor NAH-C3-GPKK was found to also potently inhibit a methyltransferase complex HemK2-Trm112 (also known as KMT9-Trm112), highlighting the importance of systematic selectivity profiling. Furthermore, this is the first potent inhibitor for HemK2/KMT9 reported until now. Thus, our studies lay the foundation for future efforts to develop selective inhibitors for either methyltransferase.With the development of endovascular technology for peripheral arterial diseases, paclitaxel drug-eluting stents and drug-coated balloons have been widely used in recent years. It has been proved that paclitaxel-coated devices have good clinical effects in reducing vascular restenosis. However, the clinical safety of paclitaxel devices has encountered challenges, some of the studies have shown that paclitaxel-coated devices may increase long-term mortality. In addition, some studies have confirmed the effectiveness and safety of paclitaxel devices, leading to this topic becoming the focus and hot spot of global attention. Whether paclitaxel-coated devices increase the risk of long-term death, whether paclitaxel doses are related to mortality, and the pharmacokinetics of paclitaxel devices should be examined.Currently,