186040-83-5

Upstream product

• 28188-41-2 m-(bromomethyl)benzonitrile 
• 153181-25-0 (4R,5S,6S,7R)-hexahydro-5,6-bis(2-methoxyethoxymethoxy)-4,7-bis(phenylmethyl)-2H-1,3-diazepin-2-one 
• 58917-85-4 N-(benzyloxycarbonyl)-D-phenylalaninol 
• 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 

Downstream Products

• 153183-11-0 (4R,5S,6S,7R)-4,7-Dibenzyl-5,6-dihydroxy-1,3-bis-(3-hydroxymethyl-benzyl)-[1,3]diazepan-2-one 
• 1053700-28-9 C₅₇H₆₀N₈O₉ 
• 1054652-60-6 C₄₉H₅₄N₆O₉S₂ 
• 1053633-47-8 C₄₉H₅₆N₈O₉ 
• 208106-02-9 C₄₃H₅₂N₄O₉ 
• 186040-84-6 (4R-(4α,5α,6β,7β))-3,3'{[tetrahydro-5,6-bis[(2-methoxyethoxy)methoxy]-2-oxo-4,7-bis(phenylmethyl)-1H-1,3-diazepine-1,3(2H)-diyl]bis(methylene)}bis(benzoic acid) 
• 188978-68-9 C₄₃H₅₀N₂O₉ 

Relevant academic research and scientific papers

Cyclic HIV protease inhibitors: Design and synthesis of orally bioavailable, pyrazole P2/P2' cyclic ureas with improved potency

Highly potent HIV-1 protease (HIVPR) inhibitors have been designed and synthesized by introducing bidentate hydrogen-bonding oxime and pyrazole groups at the meta-position of the phenyl ring on the P2/P2' substituents of cyclic ureas. Nonsymmetrical cyclic ureas incorporating 3(1H)-pyrazolylbenzyl as P2 and hydrophilic functionalities as P2' show potent protease inhibition and antiviral activities against HIV and have good oral bioavailabilities. The X-ray structure of HIVPR-10A complex confirms that the two pyrazole rings of 10A form bidentate hydrogen bonds with the side-chain oxygen (C=O) and backbone nitrogen (N-H) of Asp30/30' of HIVPR.

Cyclic urea amides: Hiv-1 protease inhibitors with low nanomolar potency against both wild type and protease inhibitor resistant mutants of HIV

Cyclic urea amides, a novel series of HIV-1 protease (HIV PR) inhibitors, have increased activity against drug-resistant mutants of the HIV PR. The design strategy for these inhibitors is based on the hypotheses that (i) the hydrogen-bonding interactions

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