24477-57-4

Upstream product

• 105-39-5 chloroacetic acid ethyl ester 
• 1193-02-8 4-aminotiophenol 
• 105-36-2 ethyl bromoacetate 
• 623-73-4 diazoacetic acid ethyl ester 

Downstream Products

• 86410-28-8 (4-Hexadecylamino-phenylsulfanyl)-acetic acid ethyl ester 
• 98594-28-6 2-((4-aminophenyl)thio)acetohydrazide 
• 86410-27-7 (4-Hexadecylamino-phenylsulfanyl)-acetic acid 

Relevant academic research and scientific papers

Chemoselective Cyclopropanation over Carbene Y-H Insertion Catalyzed by an Engineered Carbene Transferase

Hemoproteins have recently emerged as promising biocatalysts for promoting a variety of carbene transfer reactions including cyclopropanation and Y-H insertion (Y = N, S, Si, B). For these and synthetic carbene transfer catalysts alike, achieving high chemoselectivity toward cyclopropanation in olefin substrates bearing unprotected Y-H groups has proven remarkably challenging due to competition from the more facile carbene Y-H insertion reaction. In this report, we describe the development of a novel artificial metalloenzyme based on an engineered myoglobin incorporating a serine-ligated Co-porphyrin cofactor that is capable of offering high selectivity toward olefin cyclopropanation over N-H and Si-H insertion. Intramolecular competition experiments revealed a distinct and dramatically altered chemoselectivity of the Mb(H64V,V68A,H93S)[Co(ppIX)] variant in carbene transfer reactions compared to myoglobin-based variants containing the native histidine-ligated heme cofactor or other metal/proximal ligand substitutions. These studies highlight the functional plasticity of myoglobin as a "carbene transferase" and illustrate how modulation of the cofactor environment within this metalloprotein scaffold represents a valuable strategy for accessing carbene transfer reactivity not exhibited by naturally occurring hemoproteins or transition metal catalysts.

Challenging clinically unresponsive medullary thyroid cancer: Discovery and pharmacological activity of novel RET inhibitors

It is now known that “gain of function” mutations of RET (REarranged during Transfection) kinase are specific and key oncogenic events in the onset of thyroid gland cancers such as the Medullary Thyroid Carcinoma (MTC). Although a number of RET inhibitors exist and are capable of inhibiting RET variants, in which mutations are outside the enzyme active site, the majority becomes dramatically ineffective when mutations are within the protein active site (V804L and V804M). Pursuing a receptor-based virtual screening against the kinase domain of RET, we found that compound 5 is able to inhibit efficiently both wild type and V804L mutant RET. Compound 5 was able to significantly reduce proliferation of both commercially available TT cell lines and surgical thyroid tissues obtained from patients with MTC and displayed a suitable drug-like profile, thus standing out as a promising candidate for further development towards the treatment of clinically unresponsive MTC.

PPAR AGONIST COMPOUNDS, PREPARATION AND USES

The present invention relates to novel PPAR agonist compounds as well as pharmaceutical compositions containing them. The compounds according to the invention are of quite particular therapeutic interest, notably for treating diabetes and/or dyslipidemias, as well as for preventing cardiovascular pathologies.