150188-64-0

Upstream product

• 99-07-0 3-Dimethylaminophenol 
• 305129-48-0 (3-dimethylamino-phenoxy)-acetic acid benzyl ester 

Downstream Products

• 25441-20-7 2-(3-Dimethylamino-phenoxy)-N-dimethylcarbamoylmethyl-acetamide 
• 1448616-34-9 (S)-N-((S)-1-(benzo[d]thiazol-2-yl)-1-oxo-3-((S)-2-oxopyrrolidin-3-yl)propan-2-yl)-2-(2-(3-(dimethylamino)phenoxy)acetamido)-4-methylpentanamide 
• 1234189-96-8 C₁₆H₂₄N₂O₄ 
• 1448616-12-3 (S)-tert-butyl 2-(2-(3-(dimethylamino)phenoxy)acetamido)-4-methylpentanoate 
• 210181-19-4 (R)-N-tert-butyl-3-{(2S,3S)-2-hydroxy-3-[(S)-2-(3-dimethylaminophenoxyacetyl)amino-3-methylbutanoyl]amino-4-phenylbutanoyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxamide 
• 25441-19-4 2-(3-Dimethylamino-phenoxy)-N-methylcarbamoylmethyl-acetamide 

Relevant academic research and scientific papers

Design, synthesis and biological evaluation of oxime lacking Psammaplin inspired chemical libraries as anti-cancer agents

In this study, we attempted the chemical simplification of Psammaplin (PsA), while retaining its activity in vitro. Inspired by the previous Structure Activity Relationship (SAR) studies on various PsA analogues and relying on the fact that oxime is metabolically unstable, we initially designed and synthesized a diverse library of PsA analogues and evaluated for cytotoxic activity. Among 32 compounds of Psammaplin analogues synthesized, the compound 10b was almost equally active as parent Psammaplin in vitro.

Structure-activity relationship of orally potent tripeptide-based HIV protease inhibitors containing hydroxymethylcarbonyl isostere

We designed and synthesized a new class of peptidomimetic human immunodeficiency virus protease inhibitors containing a unique unnatural amino acid, allophenylnorstatine [Apns; (2S,3S)-3-amino-2-hydroxy-4-phenylbutyric acid], with a hydroxymethylcarbonyl isostere as the active moiety. From a structure-activity relationship study of HIV-1 protease inhibition, enzyme selectivity for other aspartyl proteases, the antiviral activity and pharmacokinetics in rats, 24c (KNI-227) and 24d (KNI-272, our first clinical candidate) were found to be selective and orally potent HIV protease inhibitors. Moreover, an improvement of the pharmacokinetic features of KNI-272 provided two long-lasting and highly bioavailable compounds (24g: JE-2178,h: JE-2179).