79617-27-9

Basic information

• Product Name: H-ALLO-THR-OME HCL
• Synonyms: ALLO-THREONINE-OME HCL;H-ALLO-THR-OME HCL;L-ALLO-THREONINE METHYL ESTER HYDROCHLORIDE;H-allo-Thr-OMe;(2S,3S)-Methyl 2-aMino-3-hydroxybutanoate hydrochloride
• CAS NO: 79617-27-9
• Molecular Formula: C₅H₁₁NO₃*ClH
• Molecular Weight: 169.61
• Mol File: 79617-27-9.mol

Chemical Properties

• Melting Point: 95-97 °C
• Appearance: /
• Storage Temp.: 2-8°C
• CAS DataBase Reference: H-ALLO-THR-OME HCL(CAS DataBase Reference)
• NIST Chemistry Reference: H-ALLO-THR-OME HCL(79617-27-9)
• EPA Substance Registry System: H-ALLO-THR-OME HCL(79617-27-9)

Safety Data

• Hazardous Substances Data: 79617-27-9(Hazardous Substances Data)

Usage

Uses

Used in Scientific Research:
H-ALLO-THR-OME HCL is used as a building block in the synthesis of peptides for the study of protein structures and functions. Its unique allo configuration and methoxy group provide specific properties that can be exploited in the design and development of novel bioactive peptides.
Used in Biological Applications:
H-ALLO-THR-OME HCL is utilized in various biological applications, such as enzyme inhibition studies, receptor binding assays, and the development of new therapeutic agents. Its hydrochloride salt form ensures better solubility and stability, facilitating its use in these applications.

Upstream product

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

Downstream Products

• 28415-16-9 methyl N-benzoyl (+/-)-threoninate 
• 57224-63-2 Z-DL-Thr-OMe 
• 72-19-5 L-threonine 
• 82679-55-8 D-threonine methyl ester 
• 57224-63-2 Z-DL-aThr-OMe 
• 500220-28-0 Boc-L-phenylalanine-L-threonine methyl ester 
• 17554-22-2 CBZ-Phe-Thr-OMe 
• 515-93-5 (2S,3R)-2-amino-1,3-butanediol 

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.

NOVEL COMPOUNDS AND THEIR USE

The present invention provides compounds of the general formula (I) or a pharmaceutically acceptable prodrugs, salts and/or solvates thereof, wherein LHS is selected from the group consisting of LHSa and LHSb And wherein, the asterisk (*) marks the point of attachment; These compounds exhibit antibacterial activity against Gram-negative and Gram-positive bacteria, especially S. aureus, E. coli, K. pneumoniae and A. baumannii. Pharmaceutical compositions containing these compounds, therapeutic uses thereof and methods for manufacturing the same are also provided.

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.

A Novel N-Substituted Valine Derivative with Unique Peroxisome Proliferator-Activated Receptor γbinding Properties and Biological Activities

A proprietary library of novel N-Aryl-substituted amino acid derivatives bearing a hydroxamate head group allowed the identification of compound 3a that possesses weak proadipogenic and peroxisome proliferator-Activated receptor γ(PPARI) activating properties. The systematic optimization of 3a, in order to improve its PPARγagonist activity, led to the synthesis of compound 7j (N-Aryl-substituted valine derivative) that possesses dual PPARI/PPARα agonistic activity. Structural and kinetic analyses reveal that 7j occupies the typical ligand binding domain of the PPARγagonists with, however, a unique high-Affinity binding mode. Furthermore, 7j is highly effective in preventing cyclin-dependent kinase 5-mediated phosphorylation of PPARγserine 273. Although less proadipogenic than rosiglitazone, 7j significantly increases adipocyte insulin-stimulated glucose uptake and efficiently promotes white-To-brown adipocyte conversion. In addition, 7j prevents oleic acid-induced lipid accumulation in hepatoma cells. The unique biochemical properties and biological activities of compound 7j suggest that it would be a promising candidate for the development of compounds to reduce insulin resistance, obesity, and nonalcoholic fatty liver disease.

Synthetic Access to 3-Substituted Pyroglutamic Acids from Tetramate Derivatives of Serine, Threonine, allo-Threonine, and Cysteine

A general route which provides direct access to pyroglutamates from tetramates, making use of Suzuki coupling on an enol mesylate, followed by reduction, is reported. This work permits direct scaffold hopping from tetramate to substituted pyroglutamates. Some compounds in the library showed modest antibacterial activity against Gram-positive bacteria.

Synthetic access to 3,4-disubstituted pyroglutamates from tetramate derivatives from serine, allo-threonine and cysteine

A route allowing the conversion of substituted tetramates to 3,4-disubstituted pyroglutamates, making use of Suzuki coupling on an enol mesylate, followed by reduction, is both general and fully stereoselective.

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.

Radical-mediated intramolecular β-C(sp3)-H amidation of alkylimidates: Facile synthesis of 1,2-amino alcohols

A new radical-mediated intramolecular β-C(sp3)-H amidation reaction of O-alkyl trichloro- or arylimidates is reported. Various oxazolines were efficiently prepared from easily accessible alcohol starting materials. The trichloro-oxazoline products can be hydrolyzed under mild conditions to give valuable 1,2-amino alcohols. This amidation reaction exhibits a broad substrate scope and good functional group tolerance, and offers a powerful means for the C(sp3)-H functionalization of alcohols. Mechanistic studies suggest that a sequence of 1,5-HAT of an imidate radical, iodination and cyclization might be operative.

Synthesis of sialic acid derivatives based on chiral substrate-controlled stereoselective aldol reactions using pyruvic acid oxabicyclo[2.2.2]octyl orthoester

The synthesis of sialic acids and their analogs was accomplished based on substrate-controlled asymmetric aldol reactions between sterically complicated aldehydes easily prepared from commercially available carbohydrates and a novel pyruvic acid oxabicyclo[2.2.2]octyl orthoester. Systematic aldol reaction studies using chiral aldehydes revealed that α,β,γ-benzyloxy-substituted aldehydes with an α,β-anti relative configuration preferentially provided the Felkin products with the 4,5-anti configuration with high diastereoselectivity. The relative β,γ-configuration in α,β,γ-benzyloxy-substituted aldehydes with an α,β-syn arrangement exerted a secondary effect on the diastereoselectivity of the stereogenic center formed in aldol reactions, and α,β-syn-β,γ-anti benzyloxyaldehyde exhibited superior diastereoselectivity to α,β-syn-β,γ-syn benzyloxyaldehyde to yield the Felkin products.

Dehydrodipeptide Hydrogelators Containing Naproxen N-Capped Tryptophan: Self-Assembly, Hydrogel Characterization, and Evaluation as Potential Drug Nanocarriers

In this work, we introduce dipeptides containing tryptophan N-capped with the nonsteroidal anti-inflammatory drug naproxen and C-terminal dehydroamino acids, dehydrophenylalanine (ΔPhe), dehydroaminobutyric acid (ΔAbu), and dehydroalanine (ΔAla) as efficacious protease resistant hydrogelators. Optimized conditions for gel formation are reported. Transmission electron microscopy experiments revealed that the hydrogels consist of networks of micro/nanosized fibers formed by peptide self-assembly. Fluorescence and circular dichroism spectroscopy indicate that the self-assembly process is driven by stacking interactions of the aromatic groups. The naphthalene groups of the naproxen moieties are highly organized in the fibers through chiral stacking. Rheological experiments demonstrated that the most hydrophobic peptide (containing C-terminal ΔPhe) formed more elastic gels at lower critical gelation concentrations. This gel revealed irreversible breakup, while the C-terminal ΔAbu and ΔAla gels, although less elastic, exhibited structural recovery and partial healing of the elastic properties. A potential antitumor thieno[3,2-b]pyridine derivative was incorporated (noncovalently) into the gel formed by the hydrogelator containing C-terminal ΔPhe residue. Fluorescence and F?rster resonance energy transfer measurements indicate that the drug is located in a hydrophobic environment, near/associated with the peptide fibers, establishing this type of hydrogel as a good drug-nanocarrier candidate.