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

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

Uses

Used in Pharmaceutical Research:
H-D-ALA-D-ALA-OME HCL is used as a dipeptide analogue for the development of new pharmaceutical compounds. Its unique structure and properties allow researchers to study its interactions with biological systems and explore its potential therapeutic applications.
Used in Biochemical Research:
In biochemical research, H-D-ALA-D-ALA-OME HCL is used as a model compound to investigate the behavior of dipeptides and their interactions with enzymes, receptors, and other biomolecules. This helps researchers understand the fundamental processes of peptide metabolism and signaling.
Used in Drug Design and Development:
H-D-ALA-D-ALA-OME HCL is employed as a starting point for the design and development of new drugs targeting specific biological pathways. Its unique stereochemistry and functional groups can be modified to create novel compounds with improved pharmacological properties.
Used in Analytical Chemistry:
In analytical chemistry, H-D-ALA-D-ALA-OME HCL can be used as a reference compound for the development and validation of analytical methods for the detection and quantification of dipeptides and their derivatives in biological samples.
Used in Peptide Synthesis:
H-D-ALA-D-ALA-OME HCL serves as a building block in the synthesis of larger peptides and peptide-based therapeutics. Its well-defined structure and reactivity make it a valuable component in the construction of complex peptide sequences.
Used in Drug Delivery Systems:
H-D-ALA-D-ALA-OME HCL can be incorporated into drug delivery systems to improve the bioavailability and targeting of therapeutic agents. Its unique properties may allow for the development of novel delivery platforms, such as nanoparticles or liposomes, for enhanced drug efficacy and reduced side effects.

Upstream product

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

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

Synthesis and cellular effects of novel 1,3,5-triazine derivatives in DLD and Ht-29 human colon cancer cell lines

This study provides new information on the cellular effects of 1,3,5-triazine nitrogen mustards with different peptide groups in DLD and Ht-29 human colon cancer cell lines. A novel series of 2,4,6-trisubstituted 1,3,5-triazine derivatives bearing 2-chloroethyl and oligopeptide moieties was designed and synthesized. The most cytotoxic derivative was triazine with an Ala-Ala-OMe substituent on the ring (compound 7b). This compound induced time- and dose-dependent cytotoxicity in the DLD-1 and HT-29 colon cancer cell lines. The triazine derivative furthermore induced apoptosis through intracellular signaling pathway attenuation. Compound 7b may be a candidate for further evaluation as a chemotherapeutic agent against colorectal cancer.

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.

Additivity or cooperativity: Which model can predict the influence of simultaneous incorporation of two or more functionalities in a ligand molecule?

Predicting how binding affinity responds to ligand structural modifications in structure-activity relationship studies (SAR) is a major challenge in medicinal chemistry. This is particularly true when two or more of these modifications are carried out simultaneously. In this study, we present binding affinity data from several series of thermolysin inhibitors in which simultaneous structural modifications were investigated to determine whether they are cooperative or additive. Data revealed that, while additivity is at work in some cases, cooperativity is more commonly demonstrated. Cooperativity and additivity were then correlated with ligand descriptors, such as the spacing and the topological features of the modified groups, in a manner that may provide guidance as to when each model should be utilized. Cooperativity was particularly associated with contiguous groups and small unbranched hydrophobic side chain. Additivity, on the other hand, was associated with moderately distant hydrophobic group combinations and side chain branching. Such correlations can improve the predictability of SAR studies and can provide a starting point for additional investigations that may lead to further significant enhancements in the current scoring functions.

One-pot protection-glycosylation reactions for synthesis of lipid II analogues

(2,6-Dichloro-4-methoxyphenyl)(2,4-dichlorophenyl)methyl trichloroacetimidate (3) and its polymer-supported reagent 4 can be successfully applied to a one-pot protection-glycosylation reaction to form the disaccharide derivative 7 d for the synthesis of lipid II analogues. The temporary protecting group or linker at the C-6 position and N-Troc protecting group of 7 d can be cleaved simultaneously through a reductive condition. Overall yields of syntheses of lipid II (1) and neryl-lipid II Nε-dansylthiourea are significantly improved by using the described methods. Sweet synthetic methods: A one-pot protection glycosylation reaction of the diol glycosyl acceptor is developed for synthesis of the lipid II disaccharide (see figure, Troc=2,2,2-trichloroethoxycarbonyl). Improved syntheses of lipid II and neryl-lipid II analogues are summarized.

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.

COMPOUNDS FOR AMIDE-FORMING REACTIONS

Provided herein is a compound of Formula I, that displays remarkable physicochemical properties as a peptide-coupling additive for peptide-forming reactions in water, wherein said coupling reactions proceed without measurable racemization. A method of pro

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.

A new oxyma derivative for nonracemizable amide-forming reactions in water

An Oxyma derivative, (2,2-dimethyl-1,3-dioxolan-4-yl)methyl 2-cyano-2-(hydroxyimino)acetate (2), displayed remarkable physicochemical properties as a peptide-coupling additive for peptide-forming reactions in water. Short peptides to oligopeptides could b

Transpeptidase-mediated incorporation of d-amino acids into bacterial peptidoglycan

The β-lactams are the most important class of antibiotics in clinical use. Their lethal targets are the transpeptidase domains of penicillin binding proteins (PBPs), which catalyze the cross-linking of bacterial peptidoglycan (PG) during cell wall synthesis. The transpeptidation reaction occurs in two steps, the first being formation of a covalent enzyme intermediate and the second involving attack of an amine on this intermediate. Here we use defined PG substrates to dissect the individual steps catalyzed by a purified E. coli transpeptidase. We demonstrate that this transpeptidase accepts a set of structurally diverse d-amino acid substrates and incorporates them into PG fragments. These results provide new information on donor and acceptor requirements as well as a mechanistic basis for previous observations that noncanonical d-amino acids can be introduced into the bacterial cell wall.