19094-55-4

Upstream product

• 133-91-5 3,5-diiodosalicylic acid 
• 121789-21-7 methyl 3,5-diiodo-2-methoxybenzoate 
• 74-88-4 methyl iodide 

Downstream Products

• 101495-51-6 3,5-Diiod-2-methoxybenzoylchlorid 
• 1613336-62-1 3,5-diiodo-2-methoxy-N-methyl-N-(4-phenoxyphenyl)benzamide 
• 1613336-60-9 3,5-diiodo-2-methoxy-N-(4-phenoxyphenyl)benzamide 
• 1613336-66-5 N-(4-(4-chlorophenoxy)phenyl)-3,5-diiodo-2-methoxybenzamide 
• 1613336-71-2 3,5-diiodo-2-methoxy-N-(naphthalen-2-yl)benzamide 
• 121789-50-2 2-(3,5-Diiod-2-methoxybenzoyl)-4-4-diethoxy-2-ethoxycarbonylbutansaeure-ethylester 
• 121789-49-9 3-(3,5-Diiod-2-methoxyphenyl)-2-(1-hydroxyethyliden)-3-oxopropionsaeure-ethylester 
• 121789-48-8 2-Acetyl-3-(3,5-diiod-2-methoxyphenyl)-3-hydroxy-2-acrylsaeureethylester 
• 121789-51-3 3,5-Diiod-2-methoxybenzoesaeure-ethylester 

Relevant academic research and scientific papers

INHIBITORS OF PROTEIN ARGININE DEIMINASE 1 AND METHODS OF PREPARATION AND USE THEREOF

The invention provides novel inhibitors or inactivators of protein arginine deiminase 1, pharmaceutical compositions and methods of use thereof. The invention also relates to molecular probes based on such compounds and methods of use thereof.

Halogen Bonding Increases the Potency and Isozyme Selectivity of Protein Arginine Deiminase 1 Inhibitors

Protein arginine deiminases (PADs) hydrolyze the side chain of arginine to form citrulline. Aberrant PAD activity is associated with rheumatoid arthritis, multiple sclerosis, lupus, and certain cancers. These pathologies established the PADs as therapeutic targets and multiple PAD inhibitors are known. Herein, we describe the first highly potent PAD1-selective inhibitors (1 and 19). Detailed structure–activity relationships indicate that their potency and selectivity is due to the formation of a halogen bond with PAD1. Importantly, these inhibitors inhibit histone H3 citrullination in HEK293TPAD1 cells and mouse zygotes with excellent potency. Based on this scaffold, we also developed a PAD1-selective activity-based probe that shows remarkable cellular efficacy and proteome selectivity. Based on their potency and selectivity we expect that 1 and 19 will be widely used chemical tools to understand PAD1 biology.

Dual protonophore-chitinase inhibitors dramatically affect O. Volvulus molting

The L3-stage-specific chitinase OvCHT1 has been implicated in the development of Onchocerca volvulus, the causative agent of onchocerciasis. Closantel, a known anthelmintic drug, was previously discovered as a potent and specific OvCHT1 inhibitor. As closantel is also a known protonophore, we performed a simple scaffold modulation to map out the structural features that are relevant for its individual or dual biochemical roles. Furthermore, we present that either OvCHT1 inhibition or protonophoric activity was capable of affecting O. volvulus L3 molting and that the presence of both activities in a single molecule yielded more potent inhibition of the nematode's developmental process.

Marine Bacteria, I. - Synthesis of Pentabromopseudiline, a Cytotoxic Phenylpyrrole from Alteromonas luteo-violaceus

A new synthesis of 2,3,4-tribromo-5-(3,5-dibromo-2-hydroxyphenyl)pyrrole (1a, pentabromopseudiline), an antibiotic, enzymeinhibitory and cytotoxic active constituent of the marine bacterium Alteromonas luteo-violaceus, is described.For investigation of structure-activity relationships further 2-phenylpyrroles are investigated.Key step in their synthesis is the Grignard reaction of 2-(1,3-dioxan-2-yl)ethylmagnesium bromide (9d) with benzoyl chlorides yielding γ-phenyl-γ-ketoaldehydes 24, and the Paal-Knorr cyclisation of the latter. - Key Words: Alteromonas luteo-violaceus / Bromopyrrole / Marine bacteria / Pentabromopseudiline