37712-76-8

Usage

Uses

Used in Pharmaceutical Industry:
(S)-1-acetylazetidine-2-carboxylic acid is used as a building block for the development of novel pharmaceutical compounds, particularly for neurological disorders and cancer treatment. Its unique structure and chiral properties allow for the creation of innovative drugs with potential therapeutic benefits.
Used in Chemical Industry:
(S)-1-acetylazetidine-2-carboxylic acid is used as an intermediate in the synthesis of various chemical compounds, taking advantage of its reactive functional groups and unique azetidine ring structure.
Used in Drug Development:
(S)-1-acetylazetidine-2-carboxylic acid is used as a key component in the design and synthesis of new drugs targeting neurological disorders, leveraging its potential to modulate specific biological pathways involved in these conditions.
Used in Cancer Research:
(S)-1-acetylazetidine-2-carboxylic acid is used as a compound of interest in cancer research, exploring its potential to inhibit cancer cell growth and proliferation, as well as its ability to enhance the effectiveness of existing cancer treatments.

Upstream product

• 2517-04-6 Azetidine-2-carboxylic acid 
• 75-36-5 acetyl chloride 
• 2133-34-8 (2S)-azetidine-2-carboxylic acid 
• 108-24-7 acetic anhydride 

Relevant academic research and scientific papers

Energetic contribution to both acidity and conformational stability in peptide models

The acidity of N-acyl amino acids is dependent upon the rotameric state of the amide bond. In this work we systematically investigated the acidity difference of the rotamers (ΔpKa) in the frames of various acetylated amino acids. Our results indicated a mutual interaction of two carbonyl groups of an attractive type. We observed conservative ΔpKas for acyclic amino acids (2.2-3.0 kJ mol-1), whereas in the case of alicyclic amino acids, the experimental values revealed a strong dependency on the structural context (1.5-4.4 kJ mol-1). In homologous amino acids (α-, β-, γ-, etc.), the strength of the attraction decays in an exponential fashion. Furthermore, the interaction can accumulate through a chain of amide bonds in a cascade fashion, as demonstrated by an Ac-Pro-Pro dipeptide. As a result, we demonstrate that ΔpKa is an experimental parameter to estimate increments in the carbonyl-carbonyl alignment, as determined by the amino acid or peptidyl context. This parameter is also important in understanding the roles of amino acids in both protein folding and translation in biological systems as well as their evolutionary appearance in the genetic code.

A versatile biosynthetic approach to amide bond formation

The development of versatile and sustainable catalytic strategies for amide bond formation is a major objective for the pharmaceutical sector and the wider chemical industry. Herein, we report a biocatalytic approach to amide synthesis which exploits the diversity of Nature's amide bond forming enzymes, N-acyltransferases (NATs) and CoA ligases (CLs). By selecting combinations of NATs and CLs with desired substrate profiles, non-natural biocatalytic pathways can be built in a predictable fashion to allow access to structurally diverse secondary and tertiary amides in high yield using stoichiometric ratios of carboxylic acid and amine coupling partners. Transformations can be performed in vitro using isolated enzymes, or in vivo where reactions rely solely on cofactors generated by the cell. The utility of these whole cell systems is showcased through the preparative scale synthesis of a key intermediate of Losmapimod (GW856553X), a selective p38-mitogen activated protein kinase inhibitor.

Potent, small-molecule inhibitors of human mast cell tryptase. Antiasthmatic action of a dipeptide-based transition-state analogue containing a benzothiazole ketone

Inhibitors of human mast cell tryptase (EC 3.4.21.59) have therapeutic potential for treating allergic or inflammatory disorders. We have investigated transition-state mimetics possessing a heterocycle-activated ketone group and identified in particular benzothiazole ketone (2S)-6 (RWJ-56423) as a potent, reversible, low-molecular-weight tryptase inhibitor with a Ki value of 10 nM. A single-crystal X-ray analysis of the sulfate salt of (2S)-6 confirmed the stereochemistry. Analogues 12 and 15-17 are also potent tryptase inhibitors. Although RWJ-56423 potently inhibits trypsin (Ki = 8.1 nM), it is selective vs other serine proteases, such as kallikrein, plasmin, and thrombin. We obtained an X-ray structure of (2S)-6 complexed with bovine trypsin (1.9-? resolution), which depicts inter alia a hemiketal involving Ser-189, and hydrogen bonds with His-57 and Gln-192. Aerosol administration of 6 (2R,2S; RWJ-58643) to allergic sheep effectively antagonized antigen-induced asthmatic responses, with 70-75% blockade of the early response and complete ablation of the late response and airway hyperresponsiveness.