1262981-50-9

Basic information

• Product Name: C₃₅H₄₂N₄O₁₁S
• CAS NO: 1262981-50-9
• Molecular Weight: 726.805
• Mol File: 1262981-50-9.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: C₃₅H₄₂N₄O₁₁S(CAS DataBase Reference)
• NIST Chemistry Reference: C₃₅H₄₂N₄O₁₁S(1262981-50-9)
• EPA Substance Registry System: C₃₅H₄₂N₄O₁₁S(1262981-50-9)

Safety Data

• Hazardous Substances Data: 1262981-50-9(Hazardous Substances Data)

Upstream product

• 56733-83-6 1,3-bis(N-benzyloxycarbonyl)-spectinomycin 
• 501-53-1 benzyl chloroformate 
• 7504-44-1 thiazol-4-yl acetic acid 
• 1695-77-8 spectinomycin 

Relevant articles and documents

Structure-activity relationships of spectinamide antituberculosis agents: A dissection of ribosomal inhibition and native efflux avoidance contributions

Spectinamides are a novel class of antitubercular agents with the potential to treat drug-resistant tuberculosis infections. Their antitubercular activity is derived from both ribosomal affinity and their ability to overcome intrinsic efflux mediated by the Mycobacterium tuberculosis Rv1258c efflux pump. This study explores the structure-activity relationships through analysis of 50 targeted spectinamides. Compounds are evaluated for ribosomal translational inhibition, MIC activity in Rv1258c efflux pump deficient and wild type tuberculosis strains, and efficacy in an acute model of tuberculosis infection. The results of this study show a narrow structure-activity relationship, consistent with a tight ribosome-binding pocket and strict structural requirements to overcome native efflux. Rationalization of ribosomal inhibition data using molecular dynamics simulations showed stable complex formation for halogenated spectinamides consistent with the long post antibiotic effects observed. The lead spectinamides identified in this study demonstrated potent MIC activity against MDR and XDR tuberculosis and had desirable antitubercular class specific features including low protein binding, low microsomal metabolism, no cytotoxicity, and significant reductions in bacterial burdens in the lungs of mice infected with M. tuberculosis. The structure-activity relationships detailed here emphasize the need to examine efflux-mediated resistance in the design of antituberculosis drugs and demonstrate that it is possible to overcome intrinsic efflux with synthetic modification. The ability to understand the structure requirements for this class has produced a variety of new substituted spectinamides, which may provide useful alternative candidates and promote the further development of this class.