32547-91-4Relevant academic research and scientific papers
Identification and Optimization of Mechanism-Based Fluoroallylamine Inhibitors of Lysyl Oxidase-like 2/3
Findlay, Alison D.,Foot, Jonathan S.,Buson, Alberto,Deodhar, Mandar,Jarnicki, Andrew G.,Hansbro, Philip M.,Liu, Gang,Schilter, Heidi,Turner, Craig I.,Zhou, Wenbin,Jarolimek, Wolfgang
, p. 9874 - 9889 (2019)
Lysyl oxidase-like 2 (LOXL2) is a secreted enzyme that catalyzes the formation of cross-links in extracellular matrix proteins, namely, collagen and elastin, and is indicated in fibrotic diseases. Herein, we report the identification and subsequent optimi
Synthesis and insecticidal activity in vitro and vivo of novel benzenesulfonyl derivatives based on potent target subunit H of V-ATPase
Yang, Chaofu,Li, Xiaoting,Wei, Jielu,Zhu, Feng,Gang, Fangli,Wei, Shaopeng,Zhao, Yunlong,Zhang, Jiwen,Wu, Wenjun
, p. 3164 - 3167 (2018/09/11)
Two lead compounds with benzenesulfonamide were found through virtual screening based on the 3D structure of the subunit H of V-ATPase in previous study. 74 benzenesulfonyl derivatives were synthesized and their insecticidal activities were evaluated. The derivatives with propargyl substituents exhibit excellent insecticidal activities against Mythimna separata Walker. The LD50 values of compounds A5.7 (28.0 μg·g?1) and B5.7 (36.4 μg·g?1) were significantly less than that of Celangulin V (344.0 μg·g?1). Furthermore, Isothermal Titration Calorimetry (ITC) data indicate there is a strong binding affinity between A5.7 and V-ATPase Subunit H. These results demonstrate that it is a practical way to develop pesticides targeting at H subunit of V-ATPase.
