109650-50-2

Upstream product

• 6096-81-7 dimethyl iminodiacetate 
• 103-80-0 phenylacetyl chloride 
• 39987-25-2 dimethyl iminodiacetate hydrochloride 
• 103-82-2 phenylacetic acid 

Downstream Products

• 100143-20-2 (4-imino-2-oxo-3-phenyl-pyrrolidino)-acetic acid 
• 105911-79-3 (4-hydroxy-2-oxo-3-phenyl-pyrrolidino)-acetic acid methyl ester 
• 100372-84-7 (2-oxo-3-phenyl-pyrrolidino)-acetic acid methyl ester 
• 103984-17-4 (2,4-dioxo-3-phenyl-pyrrolidino)-acetic acid 
• 107517-72-6 (2,4-dioxo-3-phenyl-pyrrolidino)-acetic acid ethyl ester 
• 105903-41-1 (2,4-dioxo-3-phenyl-pyrrolidino)-acetic acid methyl ester 

Relevant academic research and scientific papers

Preparation, characterization and biological activity of silver nanoparticles and silver(I) complex using the new compound 2,2′-(2-phenyl acetylazanediyl)diacetic acid

Silver nanoparticles (AgNPs) were prepared by the reduction of AgNO3 using 2,2′-(2-phenyl acetylazanediyl)diacetic acid in dilute aqueous Na2CO3 solution. On the other hand, the Ag(I)-complex was prepared by reacting AgNO3 with the ligand in a 1:1 M ratio. The nanoparticles and complex formed were characterized using IR, UV-Vis and 1H NMR spectroscopy, whereas thermal studies were performed for the Ag(I) complex. The particle sizes of the AgNPS were determined by scanning electron microscopy (SEM) and transmission electron microscopy (TEM). Photographs showed that the silver sol consisted of well dispersed spherical shaped nanoparticles with particle size ranging between 6.24 and 7.84 nm. A typical plasmon absorption band at 430 nm was observed for the silver nanoparticles. 2,2′-(2-phenyl acetylazanediyl)diacetic acid acted as a reducing as well as adsorbing agent in the preparation of these spherical, silver nanoparticles. Both silver nanoparticles and Ag(I) complex proved to have antibacterial as well as antifungal activities.

Structure-activity relationships of imidazole-derived 2-[ N-carbamoylmethyl-alkylamino]acetic acids, dual binders of human insulin-degrading enzyme

Insulin degrading enzyme (IDE) is a zinc metalloprotease that degrades small amyloid peptides such as amyloid-a and insulin. So far the dearth of IDE-specific pharmacological inhibitors impacts the understanding of its role in the physiopathology of Alzheimer's disease, amyloid-a clearance, and its validation as a potential therapeutic target. Hit 1 was previously discovered by high-throughput screening. Here we describe the structure-activity study, that required the synthesis of 48 analogues. We found that while the carboxylic acid, the imidazole and the tertiary amine were critical for activity, the methyl ester was successfully optimized to an amide or a 1,2,4-oxadiazole. Along with improving their activity, compounds were optimized for solubility, lipophilicity and stability in plasma and microsomes. The docking or co-crystallization of some compounds at the exosite or the catalytic site of IDE provided the structural basis for IDE inhibition. The pharmacokinetic properties of best compounds 44 and 46 were measured in vivo. As a result, 44 (BDM43079) and its methyl ester precursor 48 (BDM43124) are useful chemical probes for the exploration of IDE's role.