105328-90-3

Basic information

• Product Name: H-D-ALA-D-ALA-OME HCL
• Synonyms: H-D-ALA-D-ALA-OME HCL;H-D-Ala-D-Ala-OMe;D-ala-d-ala-oMe hcl;D-Alanine-D-alanyl-Methyl ester hydrochloride;(R)-Methyl 2-((R)-2-aMinopropanaMido)propanoate hydrochloride
• CAS NO: 105328-90-3
• Molecular Formula: C7H15ClN2O3
• Molecular Weight: 210.66
• Mol File: 105328-90-3.mol
• Article Data: 17

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: H-D-ALA-D-ALA-OME HCL(CAS DataBase Reference)
• NIST Chemistry Reference: H-D-ALA-D-ALA-OME HCL(105328-90-3)
• EPA Substance Registry System: H-D-ALA-D-ALA-OME HCL(105328-90-3)

Safety Data

• Hazardous Substances Data: 105328-90-3(Hazardous Substances Data)

Usage

General Description

H-D-ALA-D-ALA-OME HCL, also known as (3R,3'R)-N-((3aR,7aS)-2-oxoheptan-3a-yl)-3,3'-bis(phenylmethyl)dipropylamide hydrochloride, is a laboratory-used chemical compound. It is a dipeptide analogue, meaning it's used to mimic the characteristics of peptides in biochemical research. The compound belongs to a class of organic compounds known as dipeptides, which contain a sequence of exactly two alpha-amino acids joined by a peptide bond. Its systematic name suggests that it consists of two alanine (ALA) units. The "D" signifies the stereochemistry of the molecule, indicating that they are in the dextrorotatory configuration. The "OME" denotes a methoxy group, while "HCL" indicates the presence of hydrochloride. The compound is typically used in biological and pharmaceutical research.

Upstream product

• 19794-10-6 (S)-methyl 2-((S)-2-((tert-butoxycarbonyl)amino)propanamido)propanoate 
• 2483-51-4 N-[(benzyloxy)carbonyl]-L-alanyl-L-alanine methyl ester 
• 67-56-1 methanol 
• 1948-31-8 di-L-alanine 
• 923-16-0 D-alanyl-D-alanine 

Relevant articles and documents

N-Methylimidazolium chloride-catalyzed pyrophosphate formation: Application to the synthesis of Lipid i and NDP-sugar donors

N-Methylimidazolium chloride is found to catalyze a coupling reaction between monophosphates and activated phosphorous-nitrogen intermediates such as a phosphorimidazolide and phosphoromorpholidate to form biologically important unsymmetrical pyrophosphat

Asymmetric catalysis at a distance: Catalytic, site-selective phosphorylation of teicoplanin

We report three distinct, peptide-based catalysts that enable site-selective phosphorylation of three distinct hydroxyl groups within the complex glycopeptide antibiotic teicoplanin A2-2. Two of the catalysts are based on a design that capitalizes on a catalyst-substrate interaction that mimics the biological mechanism of action for teicoplanin. These catalysts are based on a dXaa-dXaa peptide motif that is known to target the teicoplanin structure in a specific manner. The third was identified through evaluation of a set of catalysts that had been developed for historically distinct projects. Each catalyst contains additional functionality designed to dispose a catalytic moiety (a nucleophilic alkylimidazole) at a different region of the glycopeptide structure. A combination of mass spectrometry and 2D-NMR spectroscopy allowed structural assignment of the distinct phosphorylated teicoplanin derivatives. Mechanistic studies are also reported that support the hypotheses that led to the discovery of the catalysts. In this manner, small molecule catalysts have been achieved that allow rational, catalytic control over reactions at sites that are separated by 11.6, 16.5, and nearly 17.7 A, based on the X-ray crystal structure of teicoplanin A2-2. Finally, we report the biological activity of the new phosphorylated teicoplanin analogs and compare the results to the natural product itself.

Substrate derived peptidic α-ketoamides as inhibitors of the malarial protease PfSUB1

Peptidic α-ketoamides have been developed as inhibitors of the malarial protease PfSUB1. The design of inhibitors was based on the best known endogenous PfSUB1 substrate sequence, leading to compounds with low micromolar to submicromolar inhibitory activity. SAR studies were performed indicating the requirement of an aspartate mimicking the P1′ substituent and optimal P1-P4length of the non-prime part. The importance of each of the P1-P4amino acid side chains was investigated, revealing crucial interactions and size limitations.

Peptide-tethered monodentate and chelating histidylidene metal complexes: Synthesis and application in catalytic hydrosilylation

The Nδ,Nε-dimethylated histidinium salt (His*) was tethered to oligopeptides and metallated to form Ir(iii) and Rh(i) NHC complexes. Peptide-based histidylidene complexes containing only alanine, Ala-Ala-His*-[M] and Ala-Ala-Ala-His*-[M] were synthesised ([M] = Rh(cod)Cl, Ir(Cp*)Cl2), as well as oligopeptide complexes featuring a potentially chelating methionine and tyrosine residue, Met-Ala-Ala-His*-Rh(cod)Cl and Tyr-Ala-Ala-His*-Rh(cod)Cl. Chelation of the methionine-containing histidylidene ligand was induced by halide abstraction from the rhodium centre, while tyrosine remained non-coordinating under identical conditions. High catalytic activities in hydrosilylation were achieved with all peptide-based rhodium complexes. The cationic S Met,CHis*-bidentate peptide rhodium catalyst outperformed the monodentate neutral peptide complexes and constitutes one of the most efficient rhodium carbene catalysts for hydrosilylation, providing new opportunities for the use of peptides as N-heterocyclic carbene ligands in catalysis.