696574-58-0

Upstream product

• 766-85-8 3-methoxy-1-iodobenzene 
• 7390-62-7 8-mercaptoadenine 
• 7390-62-7 6-amino-7,9-dihydro-8H-purine-8-thione 
• 66224-66-6 adenine 
• 15570-12-4 3-methoxybenzenethiol 
• 6974-78-3 8-bromoadenine 

Downstream Products

• 827302-39-6 C₃₅H₃₄N₅O₂PS 
• 827302-40-9 C₃₅H₃₀N₅OPS 
• 827302-38-5 C₃₄H₃₂N₅OPS 
• 521308-36-1 9-butyl-8-(3-methoxy-phenylsulfanyl)adenine 
• 827302-49-8 C₃₅H₃₀N₅O₃PS 
• 827302-48-7 C₃₅H₃₀N₅O₂PS 
• 827302-47-6 C₃₅H₃₄N₅O₄PS 
• 827302-45-4 C₃₄H₃₂N₅O₃PS 
• 827302-46-5 C₃₅H₃₄N₅O₃PS 
• 827302-44-3 C₃₄H₃₂N₅O₂PS 
• 852030-31-0 8-(3-methoxy-phenylsulfanyl)-9-pent-4-ynyl-9H-purin-6-ylamine 
• 852030-51-4 9-(2-isopropoxy-ethyl)-8-(3-methoxy-phenylsulfanyl)-9H-purin-6-ylamine 

Relevant academic research and scientific papers

Preparation of 8-(arylsulfanyl)adenines with diazonium salts under mild, aerobic conditions

(Chemical Equation Presented) 8-(Arylsulfanyl)adenines 11 were prepared in up to 75% yield by reacting the 8-thionoadenine 6 (acetic acid 3-(6-amino-8-thioxo-7,8-dihydropurin-9-yl)propyl ester) with benzenediazonium tetrafluoroborates in DMSO. Benzenediazonium ions carrying an electron-withdrawing substituent gave the highest yields. The reaction proceeded smoothly at room temperature without any base and could be performed under air atmosphere. The extremely mild conditions are compatible with a wide range of functional groups.

General Method for the Synthesis of 8-Arylsulfanyl Adenine Derivatives

We report a general method for the synthesis of 8-arylsulfanyl adenine derivatives using a mild protocol of coupling 8-mercaptoadenine with a variety of aryl iodides.

HSP90 Inhibitors Containing a Zinc Binding Moiety

The present invention relates to HSP90 inhibitors and their use in the treatment of cell proliferative diseases such as cancer. The said derivatives may further act as HDAC inhibitors.

Evaluation of 8-arylsulfanyl, 8-arylsulfoxyl, and 8-arylsulfonyl adenine derivatives as inhibitors of the heat shock protein 90

Hsp90 is a chaperone protein with important roles in maintaining transformation and in elevating the survival and growth potential of cancer cells. Currently there is an increasing interest in developing inhibitors of this protein as anticancer therapeutics. One of such inhibitors, the purine-scaffold class, has been reported to be potent and selective against Hsp90 both in vitro and in vivo models of cancer. Here, a series of 8-arylsulfanyl, -sulfoxyl, and -sulfonyl adenine members of the purine class was synthesized and evaluated as inhibitors of the chaperone. The structure-activity relationship and selectivity for tumor Hsp90 of compounds within the series is presented. Our results suggest that 8-arylsulfanyl adenine derivatives are good inhibitors of chaperone activity, whereas oxidation of the sulfides to sulfoxides or sulfones leads to compounds of decreased activity. The study identifies derivative 11v as the most potent Hsp90 inhibitor of the purine-scaffold series published to date (EC50 = 30 nM), and also as the compound of this class with highest selectivity for tumor vs normal cell Hsp90 (700 to 3000-fold). Most rewardingly, this work has allowed for the identification of Hsp90 inhibitors with selective affinities for Hsp90-client protein complexes, derivatives that may represent useful pharmacological tools in dissecting Hsp90-regulated processes.