181952-29-4

Usage

Uses

Used in Pharmaceutical Industry:
(S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-acetamidopropanoic acid is used as a building block for the synthesis of new drugs and bioactive molecules, due to its unique molecular structure and potential pharmacological properties. It is particularly valuable for researchers in the development of novel chemical compounds and pharmaceutical products.
Used in Chemical Research:
In the field of chemical research, (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-acetamidopropanoic acid is used as a valuable tool for exploring and understanding the properties and interactions of complex molecular structures. Its unique features contribute to the advancement of knowledge in chemistry and related disciplines.
Used in Drug Discovery:
(S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-acetamidopropanoic acid is employed in drug discovery processes for its potential to modulate biological processes. It is studied for its ability to act as a therapeutic agent, which could lead to the development of new treatments for various diseases and conditions.

Upstream product

• 108-24-7 acetic anhydride 
• 181954-34-7 3-amino-N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 
• 162558-25-0 N-α-tert-butoxycarbonyl-N-β-(9-fluorenylmethoxycarbonyl)-L-diaminopropionic acid 
• 20584-70-7 L-3-acetyl-amino-2-amino-propionic acid 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 

Downstream Products

• 1189038-30-9 NH₂<-Val<-Ala<-Leu<-C₁(Ac)<-Fum-Gly-Gly-Phe-OH 
• 1189038-29-6 NH₂<-Val<-Leu<-Leu<-C₁(Ac)<-Fum-Gly-Gly-Phe-OH 
• 728865-16-5 N-[(1S)-1-[(acetylamino)methyl]-2-(hydroxyamino)-2-oxoethyl]-4'-ethyl-1,1'-biphenyl-4-carboxamide 

Relevant academic research and scientific papers

CYCLIC PEPTIDE ANTIBIOTICS

Provided herein are antibacterial compounds, wherein the compounds in some embodiments have broad spectrum bioactivity. In various embodiments, the compounds act by inhibition of lipoprotein signal peptidase II (LspA), a key protein in bacteria. Pharmaceutical compositions and methods for treatment using the compounds described herein are also provided.

Antibacterial agents

no abstract published

On-bead screening of a combinatorial fumaric acid derived peptide library yields antiplasmodial cysteine protease inhibitors with unusual peptide sequences

A new class of cysteine protease inhibitors based on fumaric acid derived oligopeptides was successfully identified from a high-throughput screening of a solid-phase bound combinatorial library. As target enzymes falcipain and rhodesain were used, which play important roles in the life cycles of the parasites which cause malaria (Plasmodium falciparum) and African sleeping sickness (Trypanosoma brucei rhodesiense). The best inhibitors with unusual amino acid sequences not reported before for this type of enzyme were also fully analyzed in detail in solution. Ki values in the lower micromolar and even nanomolar region were found. Some inhibitors are even active against plasmodia and show good selectivity relative to other enzymes. Also the mechanism of action was studied and could be shown to be irreversible inhibition.

ANTIBACTERIAL AGENTS

Antibacterial compounds of formula (I) are provided, as well as stereoisomers, pharmaceutically acceptable salts, esters, and prodrugs thereof; pharmaceutical compositions comprising such compounds; methods of treating bacterial infections by the administration of such compounds; and processes for the preparation of such compounds.

Utilization of alternate substrates by the first three modules of the epothilone synthetase assembly line

The epothilones, a family of macrolactone natural products produced by the myxobacterial species Sorangium cellulosum, are of current clinical interest as antitumor agents. Inspection of the structure of the epothilones suggests a hybrid polyketide/nonribosomal peptide biosynthetic origin, and the recent sequencing of the epothilone biosynthetic gene cluster has validated this proposal. Here we have examined unnatural substrates with the first two enzymes of the biosynthetic pathway, EpoA and EpoB, to investigate the enzymatic construction of alternate heterocyclic structures and the subsequent elongation of these products by the third enzyme of the pathway, EpoC. The epothilone biosynthetic machinery can utilize serine to install an oxazole in place of a thiazole in the epothilone structure and will tolerate functionalized donor groups from the EpoA-ACP domain to produce epothilone fragments modified at the C21 position. These studies with the early enzymes of the epothilone biosynthesis cluster suggest that combinatorial biosynthesis may be a viable means for producing a variety of epothilone analogues that incorporate diversity into the heterocycle starter unit. Copyright