869487-76-3

Usage

Uses

Used in Organic Synthesis:
(S)-Benzyl (2,6-dimethyl-3-oxohept-1-en-4-yl)carbamate is used as a reagent or intermediate in the synthesis of various other compounds. Its unique structure and reactivity contribute to its utility in creating a range of products.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, (S)-benzyl (2,6-dimethyl-3-oxohept-1-en-4-yl)carbamate is used as a key intermediate for the development of new drugs. Its complex structure allows for the creation of novel molecular entities with potential therapeutic applications.
Used in Agrochemical Industry:
(S)-Benzyl (2,6-dimethyl-3-oxohept-1-en-4-yl)carbamate also finds application in the agrochemical industry, where it is utilized in the development of new pesticides. Its chemical properties make it a promising candidate for the creation of innovative and effective products in this field.

Upstream product

• 13291-18-4 isopropenylmagnesium bromide 
• 109075-73-2 benzyl (S)-[1-(N-methoxy-N-methylamino)-4-methyl-1-oxopentan-2-yl]carbamate 
• 2018-66-8 Z-Leu-OH 
• 1068-55-9 isopropylmagnesium chloride 

Downstream Products

• 1262241-20-2 C₃₄H₅₃N₅O₆ 
• 1262241-19-9 C₄₉H₆₃N₅O₈ 
• 247068-85-5 (S)-2-amino-4-methyl-1-((R)-2-methyloxiran-2-yl)pentan-1-one trifluoroacetic acid salt 
• 869487-77-4 C₁₇H₂₅NO₃ 

Relevant academic research and scientific papers

Systematic comparison of peptidic proteasome inhibitors highlights the α-ketoamide electrophile as an auspicious reversible lead motif

The ubiquitin-proteasome system (UPS) has been successfully targeted by both academia and the pharmaceutical industry for oncological and immunological applications. Typical proteasome inhibitors are based on a peptidic backbone endowed with an electrophi

HIV protease-mediated activation of sterically capped proteasome inhibitors and substrates

Strategies for selectively killing HIV-infected cells present an appealing alternative to traditional antiretroviral drugs. We show here the first example of an inactive "Trojan horse" molecule that releases a cytotoxic, smallmolecule proteasome inhibitor upon cleavage by HIV-1 protease. As a proof-of-concept strategy, the protein avidin was used to block entry of the compound into the proteasome in the absence of HIV-1 protease. We demonstrate that this strategy is also feasible without requiring an exogenous protein; a polylysine dendrimer-containing molecule is unable to enter the proteasome until cleaved by HIV-1 protease. These results demonstrate that conditional proteasome inhibitors could prove useful in the development of new tools for chemical biology and future therapeutics.