60538-18-3

Basic information

• Product Name: H-D-ALLO-THR-OME HCL
• Synonyms: H-D-allo-Threonine Methyl Ester Hydrochloride;H-D-ALLO-THR-OME HCL;H-D-allo-Thr-OMe;D(-)-allo-Threonine Methyl ester HCl;(2R,3R)-Methyl 2-amino-3-hydroxybutanoate hydrochloride;D(-)-allo-Threonine methyl ester hydrochloride
• CAS NO: 60538-18-3
• Molecular Formula: C₅H₁₁NO₃*ClH
• Molecular Weight: 169.61
• Mol File: 60538-18-3.mol
• Article Data: 21

Chemical Properties

• Melting Point: 95-97 °C
• Appearance: /
• Storage Temp.: Sealed in dry,Room Temperature
• CAS DataBase Reference: H-D-ALLO-THR-OME HCL(CAS DataBase Reference)
• NIST Chemistry Reference: H-D-ALLO-THR-OME HCL(60538-18-3)
• EPA Substance Registry System: H-D-ALLO-THR-OME HCL(60538-18-3)

Safety Data

• Hazardous Substances Data: 60538-18-3(Hazardous Substances Data)

Usage

Description

H-D-ALLO-THR-OME HCL, also known as H-D-allo-Threonine Methyl Ester Hydrochloride, is a synthetic compound derived from the naturally occurring amino acid D-allo-threonine. It is characterized by the presence of a methyl ester group and a hydrochloride counterion, which contribute to its unique chemical properties and potential applications.

Uses

Used in Pharmaceutical Industry:
H-D-ALLO-THR-OME HCL is used as a precursor in the synthesis of inhibitors targeting the hepatitis A virus 3C cysteine proteinase. This enzyme plays a crucial role in the replication and maturation of the hepatitis A virus, making it an attractive target for antiviral drug development. By incorporating H-D-ALLO-THR-OME HCL into the structure of these inhibitors, researchers can design and develop novel therapeutic agents to combat hepatitis A virus infections and potentially reduce the associated morbidity and mortality.

Upstream product

• 1487-49-6 3-hydroxybutyric acid methyl ester 
• 67-56-1 methanol 
• 72-19-5 L-threonine 
• 72-19-5 D-threonine 
• 72-19-5 DL-threonine 
• 28954-12-3 (2S,3S)-2-amino-3-hydroxybutanoic acid 
• 60143-52-4 DL-aThr*HCl 
• 72-19-5 rac-allo-threonine 
• 60143-52-4 DL-threonine hydrochloride 

Downstream Products

• 179094-66-7 (S)-2-((1S,2S)-2-Hydroxy-1-methoxycarbonyl-propylcarbamoyl)-pyrrolidine-1-carboxylic acid benzyl ester 
• 728877-98-3 (2S,3S)-methyl 3-hydroxy-2-(tritylamino)butanoate 
• 17554-22-2 CBZ-Phe-Thr-OMe 
• 57224-63-2 Z-DL-Thr-OMe 
• 153547-44-5 methyl (4R,5R)-5-methyl-2-oxo-oxazolidine-4-carboxylate 

Relevant articles and documents

(2S, 3R)-3-amino-2-hydroxy-4-phenylbutyrylamide derivative as well as preparation method and application thereof

The invention discloses a (2S, 3R)-3-amino-2-hydroxy-4-phenylbutyrylamide derivative shown as a formula (I) or an optical isomer, a diastereomer and racemate mixture and pharmaceutically acceptable salt thereof as well as a preparation method and application of the (2S, 3R)-3-amino-2-hydroxy-4-phenylbutyrylamide derivative. It is shown by comparison of results of a positive control group and a model group on lymphedema prevention experiments that the compound disclosed in the invention shows obvious anti-edema activity.

Bicyclic Lactams Derived from Serine or Cysteine and 2-Methylpropanal

Bicyclic lactams may be prepared from serine or cysteine and 2-methylpropanal; the resulting S, N -heterocycles are more stable than the corresponding O, N -heterocycles but both are synthetic intermediates capable of further elaboration.

Singlet Oxygen Photooxidation of Peptidic Oxazoles and Thiazoles

Oxazoles and thiazoles are commonly found moieties in nonribosomal peptides (NRPs) and ribosomally synthesized post-translationally modified peptides (RiPPs), which are important biomolecules present in the environment and in natural waters. From previous studies, they seem susceptible to oxidation by singlet oxygen (1O2); therefore, we designed and synthesized model oxazole- and thiazole-peptides and measured their1O2 bimolecular reaction rate constants, showing slow photooxidation under environmental conditions. We reasoned their stability through the electron-withdrawing effect of the carboxamide substituent. Reaction products were elucidated and support a reaction mechanism involving cycloaddition followed by a series of rearrangements. The first1O2 bimolecular reaction rate constant for a RiPP, the thiazole-containing peptide Aerucyclamide A, was measured and found in good agreement with the model peptide's rate constant, highlighting the potential of using model peptides to study the transformations of other environmentally relevant NRPs and RiPPs.