1053642-16-2

Upstream product

• 100-39-0 benzyl bromide 
• 153181-22-7 (4R,5S,6S,7R)-hexahydro-5,6-bis[2-(trimethylsilyl)ethoxymethoxy]-4,7-bis(phenylmethyl)-2H-1,3-diazepin-2-one 
• 153181-18-1 dibenzyl ((2R,3S,4S,5R)-1,6-diphenyl-3,4-bis((2-(trimethylsilyl)ethoxy)methoxy)hexane-2,5-diyl)dicarbamate 
• 153181-20-5 (2R,3S,4S,5R)-1,6-diphenyl-3,4-bis((2-(trimethylsilyl)ethoxy)methoxy)hexane-2,5-diamine 
• 153223-10-0 (2R,3S,4S,5R)-2,5-bis[N-(benzyloxycarbonyl)amino]-1,6-diphenyl-3,4-hexanediol 
• 120452-49-5 N-methoxy-N-methyl-(R)-N²-Cbz-phenylalaninamide 
• 41518-17-6 C₂₂H₂₅NO₆ 
• 2448-45-5 Cbz-D-Phe 
• 183814-19-9 ((1S,2R,3S,4R)-1-Benzyl-4-benzyloxycarbonylamino-2,3-dihydroxy-5-phenyl-pentyl)-carbamic acid benzyl ester 
• 63219-70-5 N-(benzyloxycarbonyl)-D-phenylalaninal 
• 58917-85-4 N-(benzyloxycarbonyl)-D-phenylalaninol 

Downstream Products

• 153223-23-5 XL₀₇₅ 

Relevant academic research and scientific papers

Preparation and structure-activity relationship of novel P1/P1'- substituted cyclic urea-based human immunodeficiency virus type-1 protease inhibitors

A series of novel P1/P1'-substituted cyclic urea-based HIV-1 protease inhibitors was prepared. Three different synthetic schemes were used to assemble these compounds. The first approach uses amino acid-based starting materials and was originally used to prepare DMP 323. The other two approaches use L-tartaric acid or L-mannitol as the starting material. The required four contiguous R,S,S,R centers of the cyclic urea scaffold are introduced using substrate control methodology. Each approach has specific advantages based on the desired P1/P1' substituent. Designing analogs based on the enzyme's natural substrates provided compounds with reduced activity. Attempts at exploiting hydrogen bond sites in the S1/S1' pocket, suggested by molecular modeling studies, were not fruitful. Several analogs had better binding affinity compared to our initial leads. Modulating the compound's physical properties led to a 10-fold improvement in translation resulting in better overall antiviral activity.

Cyclic HIV protease inhibitors: Synthesis, conformational analysis, P2/P2' structure-activity relationship, and molecular recognition of cyclic ureas

High-resolution X-ray structures of the complexes of HIV-1 protease (HIV-1PR) with peptidomimetic inhibitors reveal the presence of a structural water molecule which is hydrogen bonded to both the mobile flaps of the enzyme and the two carbonyls flanking