225233-78-3

Usage

Uses

Used in Pharmaceutical Industry:
4-Chloro-DL-hoMophenylalanine is used as a building block for the synthesis of various drugs and pharmaceuticals, contributing to the development of new therapeutic agents.
Used in Medical Research:
4-Chloro-DL-hoMophenylalanine is used as an inhibitor of certain enzymes, making it a valuable tool in studying the treatment of various medical conditions, including cancer and neurological disorders.
Used in Biochemistry and Molecular Biology Research:
4-Chloro-DL-hoMophenylalanine is used as a research tool to investigate the effects of amino acid modifications on protein structure and function, advancing our understanding of fundamental biological processes.

Upstream product

• 143-33-9 sodium cyanide 
• 75677-02-0 3-(4-chlorophenyl)propionaldehyde 
• 7116-36-1 ethyl 3-(4-chlorophenyl)propanoate 
• 90877-70-6 ethyl 2-acetamido-2-cyanoacetate 
• 773837-37-9 sodium cyanide 
• 24393-52-0 ethyl (E)-3-(4-chlorophenyl)prop-2-enoate 
• 6282-88-8 3-(p-chlorophenyl)propanol 

Downstream Products

• 111-85-3 n-chlorooctane 
• 131403-00-4 2-Amino-4-(4-chloro-phenyl)-butyric acid octyl ester; hydrochloride 
• 917247-90-6 rac-2-hydroxy-4-(4-chlorophenyl)butanoic acid 

Relevant academic research and scientific papers

NEW TRPA1 ANTAGONISTS

The present invention relates to compounds of Formula (I), to the process for preparing such compounds and to their use in the treatment of a pathological condition or disease susceptible to amelioration by TRPA1 channel inhibition or antagonism.

Changing the selectivity profile–from substrate analog inhibitors of thrombin and factor Xa to potent matriptase inhibitors

The type II transmembrane serine protease matriptase is a potential target for anticancer therapy and might be involved in cartilage degradation in osteoarthritis or inflammatory skin disorders. Starting from previously described nonspecific thrombin and factor Xa inhibitors we have prepared new noncovalent substrate-analogs with superior potency against matriptase. The most suitable compound 35 (H-d-hTyr-Ala-4-amidinobenzylamide) binds to matriptase with an inhibition constant of 26 nM and has more than 10-fold reduced activity against thrombin and factor Xa. The crystal structure of inhibitor 35 was determined in the surrogate protease trypsin, the obtained complex was used to model the binding mode of inhibitor 35 in the active site of matriptase. The methylene insertion in d-hTyr and d-hPhe increases the flexibility of the P3 side chain compared to their d-Phe analogs, which enables an improved binding of these inhibitors in the well-defined S3/4 pocket of matriptase. Inhibitor 35 can be used for further biochemical studies with matriptase.

Biocatalytic racemization of (hetero)aryl-aliphatic α- hydroxycarboxylic acids by Lactobacillus spp. proceeds via an oxidation-reduction sequence

The biocatalytic racemization of a range of (hetero)aryl- and (di)aryl-aliphatic α-hydroxycarboxylic acids has been achieved by using whole resting cells of Lactobacillus spp. The essentially mild (physiological) reaction conditions ensure the suppression of undesired side reactions, such as elimination, decomposition or condensation. Cofactor/inhibitor studies using a cell-free extract of Lactobacillus paracasei DSM 20207 reveal that the addition of redox cofactors (NAD+/NADH) leads to a distinct increase in the racemization rate, while strong inhibition is observed in the presence of Thio-NAD+, which suggests that the racemization proceeds by an oxidation-reduction sequence rather than involvement of a "racemase" enzyme. Wiley-VCH Verlag GmbH & Co. KGaA, 2006.