152169-60-3

Usage

Uses

Used in Pharmaceutical Synthesis:
BENZYL [(1S)-1-METHYL-2-OXOPROPYL]CARBAMATE is used as an intermediate in the synthesis of (R)-1,1-Diethoxy-2-propanamine (D442115) for the development of N-protected α-amino aldehydes. These aldehydes are essential as C-terminal units in peptide aldehydes, which exhibit enzyme inhibitor activity, such as Leupeptin.
Used in Enzyme Inhibition:
In the pharmaceutical industry, BENZYL [(1S)-1-METHYL-2-OXOPROPYL]CARBAMATE is used as a key component in the synthesis of enzyme inhibitors. These inhibitors are vital for modulating various biological processes and have potential applications in the treatment of various diseases.
Used in Amino Sugar Preparation:
BENZYL [(1S)-1-METHYL-2-OXOPROPYL]CARBAMATE is also utilized in the preparation of amino sugars, which are essential components in the synthesis of various biologically active molecules, including antibiotics and antifungal agents.
Used in Unusual Amino Acid Synthesis:
Furthermore, BENZYL [(1S)-1-METHYL-2-OXOPROPYL]CARBAMATE is employed in the synthesis of unusual amino acids, which are crucial for the development of novel pharmaceutical compounds with unique properties and potential therapeutic applications.

Upstream product

• 26607-51-2 N-benzyloxycarbonyl-D-alanine 
• 6638-79-5 N,O-dimethylhydroxylamine*hydrochloride 
• 102988-93-2 C₁₆H₂₁NO₆ 

Downstream Products

• 1332641-56-1 (R)-benzyl 3-oxopent-4-en-2-ylcarbamate 
• 1332641-60-7 ethyl 2-((R)-2-(benzyloxycarbonylamino)propanoyl)-cyclopropanecarboxylate 
• 1332768-39-4 ethyl 2-((2R)-2-(benzyloxycarbonylamino)-1-hydroxypropyl)-cyclopropanecarboxylate 
• 1332641-61-8 (1S)-benzyl 2-[2-(ethoxycarbonyl)cyclopropanecarbonyl]pyrrolidine-1-carboxylate 
• 1332768-38-3 (1S)-benzyl 2-[(2-(ethoxycarbonyl)cyclopropyl)(hydroxy)methyl]pyrrolidine-1-carboxylate 
• 1609345-44-9 benzyl [(2R)-3-oxobutan-2-yl]carbamate 
• 177283-75-9 dibenzyl ((2R,3S,4S,5R)-3,4-bis((2-(trimethylsilyl)ethoxy)methoxy)hexane-2,5-diyl)dicarbamate 
• 177283-74-8 dibenzyl ((2R,3S,4S,5R)-3,4-dihydroxyhexane-2,5-diyl)dicarbamate 
• 105499-10-3 (R)-benzyl-(1-methyl-2-oxoethyl)carbamate 

Relevant academic research and scientific papers

Amino-substituted imidazo[1,2-a]pyridinecarboxamides and their use

The present application relates to novel substituted imidazo[1,2-a]pyridine-3-carboxamides, to processes for their preparation, to their use alone or in combinations for the treatment and/or prophylaxis of diseases and to their use for preparing medicaments for the treatment and/or prophylaxis of diseases, in particular for the treatment and/or prophylaxis of cardiovascular disorders.

Three-step synthesis of cyclopropyl peptidomimetics

An efficient approach to novel cyclopropyl peptidomimetics has been developed. The synthetic route involves a cyclopropanation using ethyl (dimethylsulfuranylidene)acetate (EDSA) as the key step and affords a cyclopropyl peptidomimetic core in three steps

CYCLIC DIARYL ETHER COMPOUNDS AS ANTAGONISTS OF PROSTAGLANDIN D2 RECEPTORS

Described herein are compounds that are antagonists of PGD2 receptors. Also described are pharmaceutical compositions and medicaments that include the antagonists of PGD2 receptors described herein, as well as methods of using such antagonists of PGD2 receptors, alone and in combination with other compounds, for treating respiratory, cardiovascular, and other PGD2-dependent or PGD2-mediated conditions or diseases.

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.