19641-83-9

Usage

Uses

Used in Pharmaceutical Industry:
(RS)-3,5-DHPG is used as a therapeutic agent for the treatment of Parkinson's disease. It acts as a potential target in modulating the underlying neurochemical changes associated with the disease, offering a promising avenue for symptom management and disease progression.
Used in Neurochemical Research:
(RS)-3,5-DHPG is used as a research tool for studying the role of metabotropic glutamate receptors in various neurological processes. Its ability to modulate Kir4.1 protein and mRNA in cultured rat retinal Müller cells makes it a valuable compound for understanding the intricate mechanisms of neuronal communication and potential therapeutic interventions.
Used in Drug Development:
(RS)-3,5-DHPG serves as a lead compound in the development of new drugs targeting group I metabotropic glutamate receptors. Its agonistic properties can be leveraged to design novel therapeutics for a range of neurological and psychiatric disorders, including Parkinson's disease, epilepsy, and anxiety disorders.

Biological Activity

Selective group I metabotropic glutamate receptor agonist which activates both mGlu 1 and mGlu 5 . Also reported to be an antagonist at metabotropic glutamate receptors linked to phospholipase D.

InChI:InChI=1/C8H9NO4/c10-6-1-5(2-7(11)3-6)9-4-8(12)13/h1-3,9-11H,4H2,(H,12,13)

Upstream product

• 187978-82-1 5-(3',5'-dihydroxyphenyl)hydantoin 
• 116435-46-2 5-(3,5-Dimethoxy-phenyl)-imidazolidine-2,4-dione 
• 1208237-23-3 2-amino-2-(3,5-dihydroxyphenyl)acetonitrile 
• 7311-34-4 3,5-dimethoxybenzaldehdye 
• 187979-09-5 (R)-(3,5-Dihydroxy-phenyl)-ureido-acetic acid 

Downstream Products

• 1598416-01-3 Fmoc-D-Dpg-OH 

Relevant academic research and scientific papers

Large α-aminonitrilase activity screening of nitrilase superfamily members: Access to conversion and enantiospecificity by LC-MS

A high-throughput screening for the identification of nitrilases demonstrating activity towards alpha-aminonitriles is reported. A LC-MS assay giving access to both conversion and enantiospecificity was developed. 588 candidate enzymes were screened as cell lysates against six alpha-aminonitriles in 96-well microplates. The candidate enzymes were selected following two criteria, their sequence identity with a set of known nitrilases or their phylogenetic position among the nitrilase superfamily. Five enzymes were identified and found to hydrolyse alpha-aminonitrile into the corresponding alpha-aminoacid. The substrate range was found to be very narrow as only two different alpha-aminonitriles, 2-aminovaleronitrile and 2-amino-2- phenylacetonitrile, were found to be substrates. The biocatalytic capabilities of three enzymes were further investigated and the best result was obtained with an enzyme from Burkholderia xenovorans catalysing the enantiospecific hydrolysis of 2-aminovaleronitrile into (S)-norvaline with excellent conversion and enantiomeric excess.

Production of ring-substituted D-phenylglycines by microbial or enzymatic hydrolysis/deracemisation of the corresponding DL-hydantoins

A series of 17 ring-mono and -disubstituted D-phenylglycine derivatives was prepared in high enantiomeric purity by enzymatic hydrolysis and deracemisation of the corresponding DL-hydantoins, using D-hydantoinase activities of microorganisms or purified enzymes, followed by diazotation of the resulting N-carbamyl-D-amino acids. No significant L-hydantoinase activity was found to produce the corresponding L-enantiomers.

New antiviral antibiotics, kistamicins A and B. II. Structure determination

The structures of antiviral antibiotics kistamicins A and B have been determined by a combination of chemical degradation and spectral analysis. They are commonly composed of D-tyrosine 3,5-dihydrophenylglycine a biphenyl ether bis-amino acid and a diphenyl substituted indole tris-amino acid forming a tricyclic ring structure. Kistamicin B possessed a phenethylamide at the amino terminal of kistamicin A. They are structurally related to the nuclei of the vancomycin group antibiotics particularly to antibiotic complestatin.