194801-63-3

Basic information

• Product Name: ADIPIC BIS((3-NITROBENZYLIDENE)HYDRAZIDE)
• Synonyms: ADIPIC BIS((3-NITROBENZYLIDENE)HYDRAZIDE)
• CAS NO: 194801-63-3
• Molecular Formula: C₂₀H₂₀N₆O₆
• Molecular Weight: 440.4094
• Mol File: 194801-63-3.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• CAS DataBase Reference: ADIPIC BIS((3-NITROBENZYLIDENE)HYDRAZIDE)(CAS DataBase Reference)
• NIST Chemistry Reference: ADIPIC BIS((3-NITROBENZYLIDENE)HYDRAZIDE)(194801-63-3)
• EPA Substance Registry System: ADIPIC BIS((3-NITROBENZYLIDENE)HYDRAZIDE)(194801-63-3)

Safety Data

• Hazardous Substances Data: 194801-63-3(Hazardous Substances Data)

Upstream product

• 99-61-6 3-nitro-benzaldehyde 
• 1071-93-8 adipic acid dihydrazide 

Relevant articles and documents

Bivalent enzyme inhibitors discovered using dynamic covalent chemistry

A bivalent dynamic covalent chemistry (DCC) system has been designed to selectively target members of the homodimeric glutathione-S-transferase (GST) enzyme family. The dynamic covalent libraries (DCLs) use aniline-catalysed acylhydrazone exchange between bivalent hydrazides and glutathione-conjugated aldehydes and the bis-hydrazides act as linkers to bridge between each glutathione binding site. The resultant DCLs were found to be compatible and highly responsive to templating with different GST isozymes, with the best results coming from the M and Schistosoma japonicum (Sj) class of GSTs, targets in cancer and tropical disease, respectively. The approach yielded compounds with selective, nanomolar affinity (Ki=61 nM for mGSTM1-1) and demonstrates that DCC can be used to simultaneously interrogate binding sites on different subunits of a dimeric protein. Library powers: A bivalent dynamic covalent chemistry (DCC) system has been designed to selectively target members of the homodimeric glutathione-S-transferase (GST) enzyme family. The approach (see scheme) yielded compounds with selective, nanomolar affinity and demonstrates that DCC can be used to simultaneously interrogate binding sites on different subunits of a dimeric protein. Copyright