1187225-45-1

Basic information

• Product Name: 4-iodo-N-(4-chlorobut-2-ynyl)-benzenesulfonamide
• Synonyms: 4-iodo-N-(4-chlorobut-2-ynyl)-benzenesulfonamide
• CAS NO: 1187225-45-1
• Molecular Weight: 369.61
• Mol File: 1187225-45-1.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: 4-iodo-N-(4-chlorobut-2-ynyl)-benzenesulfonamide(CAS DataBase Reference)
• NIST Chemistry Reference: 4-iodo-N-(4-chlorobut-2-ynyl)-benzenesulfonamide(1187225-45-1)
• EPA Substance Registry System: 4-iodo-N-(4-chlorobut-2-ynyl)-benzenesulfonamide(1187225-45-1)

Safety Data

• Hazardous Substances Data: 1187225-45-1(Hazardous Substances Data)

Upstream product

• 98-61-3 p-Iodobenzenesulfonyl chloride 
• 77369-59-6 1-Amino-4-chloro-2-butyne hydrochloride 

Downstream Products

• 1187225-48-4 N-(4-azidobut-2-ynyl)-4-iodobenzenesulfonamide 

Relevant articles and documents

Structural studies of triazole inhibitors with promising inhibitor effects against antibiotic resistance metallo-β-lactamases

Metallo-β-lactamases (MBLs) are an emerging cause of bacterial antibiotic resistance by hydrolysing all classes of β-lactams except monobactams, and the MBLs are not inhibited by clinically available serine-β-lactamase inhibitors. Two of the most commonly encountered MBLs in clinical isolates worldwide – the New Delhi metallo-β-lactamase (NDM-1) and the Verona integron-encoded metallo-β-lactamase (VIM-2) – are included in this study. A series of several NH-1,2,3-triazoles was prepared by a three-step protocol utilizing Banert cascade reaction as the key step. The inhibitor properties were evaluated in biochemical assays against the MBLs VIM-2, NDM-1 and GIM-1, and VIM-2 showed IC50 values down to nanomolar range. High-resolution crystal structures of four inhibitors in complex with VIM-2 revealed hydrogen bonds from the triazole inhibitors to Arg228 and to the backbone of Ala231 or Asn233, along with hydrophobic interactions to Trp87, Phe61 and Tyr67. The inhibitors show reduced MIC in synergy assays with Pseudomonas aeruginosa and Escherichia coli strains harbouring VIM enzymes. The obtained results will be useful for further structural guided design of MBL inhibitors.

Inhibitors of VIM-2 by screening pharmacologically active and click-chemistry compound libraries

VIM-2 is an Ambler class B metallo-β-lactamase (MBL) capable of hydrolyzing a broad-spectrum of β-lactam antibiotics. Although the discovery and development of MBL inhibitors continue to be an area of active research, an array of potent, small molecule in