Hypervalent Organoiodine Promoted Dearylation Reaction of N-Aryl Sulfonamides
CHINESE JOURNAL OF ORGANIC CHEMISTRY
Authors: Song Mengmeng; Zhang Zhiguo; Zheng Dan; Li Xiang; Liang Rui; Zhao Xu'na; Shi Lei; Zhang Guisheng
Abstract
An efficient Dess-Martin periodinane (DMP)-promoted dearylation of N-arylsulfonamides was developed through a highly selective oxidative cleavage of the inert C(aryl)-N bonds in secondary sulfonamides while leaving the S-N bond unchanged. This metal-free reaction proceeds under mild conditions and provides access to various biologically important primary sulfonamides, some of which are otherwise unattainable using conventional aminolysis and hydrolysis methods. The concise and efficient dearylation reaction provides the use of an aryl group as a removable protecting sulfonamide group under metal catalyst-free conditions.
In Vitro, Molecular Docking, and In Silico Binding Mode Analysis of Organic Compounds for Antimicrobial and Anticancer Activity against Jurkat, HCT116, and A549 Cell Lines.
CHEMISTRYSELECT
Authors: Naha, Sanay; Govindaiah, Shivaraja; Sreenivasa, Swamy; Prakash, Jeevan Kallur; Velmathi, Sivan
Abstract
A set of four novel organic molecules bearing hydrazide, azomethine, and sulfonamide linkages were synthesized by a condensation reaction, and characterized using ubiquitous spectroscopic techniques. The synthesized molecules were screened against Jurkat, HCT116, and A549 cell lines for their in-vitro cytotoxic activity, antimicrobial activity and were found to be promising as anticancer and antimicrobial agents. Among four molecules, pyridine-hydroxynaphalene based molecule (R3) showed comprehensive anticancer activity towards all three cancer cell lines. On the other hand, R1, R2, and R4 were found to be moderate antimicrobial agents. The mode of action for anticancer activity and antimicrobial activity was further supported by molecular docking studies of the potent compounds against the enzyme Methinonyl-TRNA Synthetase (PDB ID:1PG2), bacterial DNA Gyrase B (PDB ID:3G75), and yeast GTPase (PDB ID:3 A58). Further, Molecular dynamics (MD) simulations studies were analyzed to study the stability of the ligand-protein complex.