2645-36-5Relevant articles and documents
Hydroamination and Hydrophosphination of Isocyanates/Isothiocyanates under Catalyst-Free Conditions
Zhu, Xiancui,Xu, Mengchen,Sun, Jinrong,Guo, Dianjun,Zhang, Yiwei,Zhou, Shuangliu,Wang, Shaowu
, p. 5213 - 5218 (2021/10/19)
Symmetrical and unsymmetrical N,N’-disubstituted as well as trisubstituted ureas/thioureas by the hydroamination of isocyanates/isothiocyanates, and various phosphathioureas by the hydrophosphination of isothiocyanates have been synthesized in good to excellent yields under catalyst-free and mild conditions. This protocol is also applicable for the efficient synthesis of chiral ureas and thioureas and common herbicides, such as fenuron and monuron.
Lanthanum(III) Trifluoromethanesulfonate Catalyzed Direct Synthesis of Ureas from N-Benzyloxycarbonyl-, N -Allyloxycarbonyl-, and N -2,2,2-Trichloroethoxycarbonyl-Protected Amines
Bui, Tien Tan,Kim, Hee-Kwon
supporting information, p. 997 - 1002 (2020/06/17)
A novel lanthanum triflate mediated conversion of N -benzyloxycarbonyl-, N -allyloxycarbonyl-, and N -trichloroethoxycarbonyl-protected amines into nonsymmetric ureas was discovered. In this study, lanthanum triflate was found to be an effective catalyst for preparing various nonsymmetric ureas from protected amines. A variety of protected aromatic and aliphatic carbamates reacted readily with various amines in the presence of lanthanum triflate to generate the desired ureas in high yields. This result demonstrated that this novel lanthanum triflate catalyzed preparation of ureas from Cbz, Alloc, and Troc carbamates can be employed for the formation of various urea structures.
Biochemical and microbiological evaluation of: N-aryl urea derivatives against mycobacteria and mycobacterial hydrolases
Vartak, Abhishek,Goins, Christopher,De Moura, Vinicius Calado Nogueira,Schreidah, Celine M.,Landgraf, Alexander D.,Lin, Boren,Du, Jianyang,Jackson, Mary,Ronning, Donald R.,Sucheck, Steven J.
, p. 1197 - 1204 (2019/07/25)
A focused library of 24 N-aryl urea derivatives was prepared and evaluated against serine esterases of Mycobacterium tuberculosis (Mtb) Rv3802c and Mtb Ag85C. The members of the library were evaluated for both selectivity and mode of inhibition. Furan-bas