41036-19-5

Basic information

• Product Name: H-ALA-ALA-OME HCL
• Synonyms: H-ALA-ALA-OME HCL;L-ALANYL-L-ALANINE METHYL ESTER HCL;L-ALANYL-L-ALANINE METHYLESTER HCI;H-Ala-Ala-OMe;Ala-Ala-OMe·HCL;(S)-Methyl 2-((S)-2-aMinopropanaMido)propanoate hydrochloride;Alanylalanine methyl ester hydrochloride;Methyl L-alanyl-L-alaninate monohydrochloride
• CAS NO: 41036-19-5
• Molecular Formula: C₇H₁₄N₂O₃*ClH
• Molecular Weight: 210.66
• Mol File: 41036-19-5.mol

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: H-ALA-ALA-OME HCL(CAS DataBase Reference)
• NIST Chemistry Reference: H-ALA-ALA-OME HCL(41036-19-5)
• EPA Substance Registry System: H-ALA-ALA-OME HCL(41036-19-5)

Safety Data

• Hazardous Substances Data: 41036-19-5(Hazardous Substances Data)

Usage

Chemical Properties

White powder

Upstream product

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

Downstream Products

• 73958-17-5 <1-(Biphenyl-4-yl)-1-methylethoxycarbonyl>-alanyl-alanyl-alanin-methylester 
• 1078719-18-2 C₂₉H₃₆N₄O₇ 
• 1078719-19-3 C₂₉H₃₆N₄O₇ 
• 1429338-47-5 Boc-Tyr-Ala-Ala-OMe 
• 66494-28-8 Boc-Met-Ala-Ala-OMe 
• 1429338-43-1 C₂₂H₃₆N₆O₇ 
• 1407151-30-7 Boc-Met-Ala-Ala-OH 
• 160480-13-7 Boc-Tyr-Ala-Ala-OH 

Relevant articles and documents

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.

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.

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.

Syntheses of the P-methylase substrates of the bialaphos biosynthetic pathway

(Chemical Equation Presented) Genetic studies suggest that either N-acetyldemethyl phosphinothricin (1, N-AcDMPT) or N-acetyldemethyl phosphinothricin tripeptide (2, N-AcDMPTT) is the substrate for the P-methylation reaction in the biosynthesis of phosphinothricin tripeptide (PTT), which is widely used as an herbicide. To study the mechanism for this unique P-methylation reaction catalyzed by the BcpD protein and the functions of the unusual nonribosomal peptide synthetases involved in PTT biosynthesis, this work reports the chemical syntheses of 1 and 2.

Peptidyl epoxides extended in the P′ direction as cysteine protease inhibitors: Effect on affinity and mechanism of inhibition

Endo peptidyl epoxides, in which the central epoxidic moiety replaces the scissile amide bond of a P3-P3′ peptide, were designed as cysteine proteases inhibitors. The additional P′-S′ interactions, relative to those of an exo peptidyl epoxide of the same P3-P1 sequence, significantly improved affinity to the enzymes papain and cathepsin B, but also changed the mode of inhibition from active-site directed inactivation to reversible competitive inhibition. Computational models rationalize the binding affinity and the inhibition mechanism.

Intramolecular ligation of carbonyl oxygen to central zinc in synthetic oligopeptide-linked zinc-porphyrins

Oligopeptide-linked zinc-porphyrins were prepared (oligopeptide = -Phe(m)-Ala(n)-OMe and porphyrin = 5,15-diaryl-2,3,7,8,12,13,17,18-octaethylporphyrin). 1H NMR, IR, visible, and CD spectra of the synthetic molecule in a chlorinated methane (CDCl3 or CH2Cl2) showed that the carbonyl oxygen of the N-terminal amino acid of the linked peptide should ligate the central zine metal in the molecule as the axial ligand to form a pentacoordinated zinc-porphyrin. The coordination of the zinc with the peptide framework changed the optical and electrical properties, indicating that such ligation might control the reactivity in biological metallotetrapyrrole-protein systems as well as the coordination to the peptide residue.

Amino acids and peptides. XXIII. Synthesis of N alpha-protected amino acid 6-chloro-2-pyridyl esters and their evaluation for peptide synthesis.

6-Chloro-2-pyridyl esters (OPyCl) of N alpha-benzyloxycarbonyl and tert-butyloxycarbonylamino acids were synthesized by the N,N'-dicyclohexylcarbodiimide (DCC) method from the acids and 6-chloro-2-hydroxypyridine in dimethylformamide (DMF). The reactivity of the 6-chloro-2-pyridylester with amino group is much higher than that of the corresponding 2-pyridyl ester (OPy) and p-nitrophenyl esters (ONp) in dioxane and DMF, and a peptide bond is formed without acylation at the side chain hydroxyl group of amino acids. Z-Asp(OBzl)-OPyCl reacted with amino acid methyl esters in dioxane to give the corresponding dipeptide without any detectable aspartimide formation.

Thermitase - A Thermostable Serine Protease. I. Synthesis of Alanine Peptide Esters as Substrates of the Enzyme

The synthesis of N-acetylated and N-succinylated peptide esters of alanine is described.The peptides are built up from the Z-protected peptides by liquid phase fragment condensation and by acylation of the deprotected peptide esters.The kinetic parameters Km and kcat of some compounds are presented.