N-Me-Ala-OMe
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N-Me-Ala-OMe

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Category
L-Amino Acids
Catalog number
BAT-015300
CAS number
35023-55-3
Molecular Formula
C5H11NO2
Molecular Weight
117.15
N-Me-Ala-OMe
IUPAC Name
methyl (2S)-2-(methylamino)propanoate
Synonyms
N-Me-L-Ala-OMe; N-methyl-L-alanine methyl ester; (S)-methyl 2-(methylamino)propanoate; N-methyl-(S)-alanine methylester; methyl N-methyl-L-alaninate; L-Alanine, N-methyl-, methyl ester
Related CAS
20045-77-6 (monohydrochloride)
Appearance
White Powder
Purity
98%
Density
0.946±0.06 g/cm3 (Predicted)
Boiling Point
131.3±23.0°C (Predicted)
Storage
Store at -20°C
Solubility
Soluble in Methanol
InChI
InChI=1S/C5H11NO2/c1-4(6-2)5(7)8-3/h4,6H,1-3H3/t4-/m0/s1
InChI Key
PQIUHUKRJAOTLS-BYPYZUCNSA-N
Canonical SMILES
CC(C(=O)OC)NC

N-Me-Ala-OMe, also referred to as N-Methylalanine methyl ester, stands as a versatile peptide derivative extensively employed in biochemical and pharmaceutical research. Here are the key applications of N-Me-Ala-OMe, presented with high perplexity and burstiness:

Peptide Synthesis: Serving as a foundational component in peptide and peptidomimetic synthesis, N-Me-Ala-OMe assumes a pivotal role in altering the physical and chemical attributes of peptides. This modification augments the peptides' resilience against enzymatic degradation, hence amplifying the stability of peptide-based medications and potentially enhancing their therapeutic efficacy.

Enzyme Inhibition Studies: Within the domain of enzymological inquiries, N-Me-Ala-OMe acts as a valuable instrument for exploring the inhibition mechanisms of diverse proteases. By integrating this methylated derivative into peptide sequences, researchers can delve into how subtle modifications impact the interactions between enzymes and peptides. These revelations are fundamental for designing precise protease inhibitors with promising therapeutic potentials.

Structure-Activity Relationship (SAR) Studies: In the realm of medicinal chemistry, N-Me-Ala-OMe emerges as a pivotal player in investigating the structure-activity relationships of peptides. Methylation at the nitrogen site can influence the peptide's affinity for receptors or other target proteins. Through systematic manipulations in peptide sequences and scrutiny of biological responses, researchers can pinpoint the vital structural components responsible for the peptide's activity.

Drug Delivery Systems: Embracing cutting-edge innovations, N-Me-Ala-OMe finds utility in enhancing peptide-based drug delivery systems to optimize their pharmacokinetic profiles. The inclusion of the methyl ester group can bolster membrane permeability and augment the oral bioavailability of peptide drugs. This modification harbors the potential to advance more efficient delivery platforms for therapeutic peptides, heralding new frontiers in drug delivery within the pharmaceutical landscape.

1. Enhanced cleavage of diaminopimelate-containing isopeptides by leucine aminopeptidase and matrix metalloproteinases in tumors: application to bioadhesive peptides
Y Yamazaki, M Savva, H K Kleinman, S Oka, M Mokotoff J Pept Res. 1999 Feb;53(2):177-87. doi: 10.1034/j.1399-3011.1999.00021.x.
We prepared (2S,6S)-Z-Dpm(Z)(OMe) (4) by protease-mediated hydrolysis of (R,R/S,S)-Z-Dpm(Z)(OMe)-OMe (3), converted it to (2S,6S)-Dpm(Z)(OMe) (6) via PCI5 to an NCA intermediate and hydrolysis, protected the amino group with Boc to give (2S,6S)-Boc-Dpm(Z)(OMe) (7), which upon ammonolysis of the Me ester afforded (2S,6S)-Boc-Dpm(Z)(NH2) (8). Hydrogenolysis of 8 and protection with Fmoc gave (2S,6S)-Boc-Dpm(Fmoc)(NH2)(10). Using 10 and SPPS, we prepared three Dpm-containing peptides and their corresponding Lys peptides. Enzymatic studies with mLAP and cLAP showed that the Leu moiety in Ac-Gly-(2S,6S)-Dpm(Leu)(NH2)-Ala (14) was hydrolyzed 68-fold and >1000-fold more rapidly, respectively, than that in Ac-Gly-Lys(Leu)-Ala (12). The enhanced rate of Leu formation from 14 compared to 12 was also observed with homogenates of mouse C3 sarcomas. This homogenate also hydrolyzed Ac-Gly-(2S,6S)-Dpm(Ac-Gly-Pro-Gln-Gly-Leu)(NH2)-Ala (16) to Ac-Gly-(2S,6S)-Dpm(NH2)-Ala (13), Leu and Ac-Gly-Pro-Gln-Gly (17). This implies the side chain is cleaved first by endopeptidases, such as matrix metalloproteinases (MMPs), and then the remaining Leu is cleaved by LAP-like exopeptidases. The rate of liberation of 17 from 16 and the corresponding Lys isopeptide, Ac-Gly-Lys(Ac-Gly-Pro-Gln-Gly-Leu)-Ala (15), was not significantly different. The rate of formation of 13 was faster from 16 than Ac-Gly-Lys-Ala (11) was from 15. Thus, the entire isopeptide side chain can be removed by the cooperative action of LAP-like and MMP-like peptidases present in tumor tissue, which occurs faster in the Dpm peptide 16 than in the Lys peptide 15. The rate of formation of 13 from 16 by lung, liver, and intestine homogenates (from the same C3 tumor-bearing mice) was comparable to or higher than from the tumor homogenates, but the rate by blood was only 4% the value of the tumor homogenates. Analogs of a bioadhesive fragment from the laminin alpha1 chain were prepared by replacing the essential Lys with Dpm(NH2) (20) and Dpm(Leu)(NH2) (21). Both Dpm-containing peptides were active, although considerably weaker than the corresponding Lys peptides 18 and 19, in a cell attachment assay with human fibrosarcoma HT-1080 cells.
2. Mechanism of action of papain: aryldehydroalanines as spectroscopic probes of acyl enzyme formation
M Smolarsky Biochemistry. 1978 Oct 31;17(22):4606-15. doi: 10.1021/bi00615a005.
The alpha,beta-unsaturated aromatic amino acids phenyldehydroalanine (PDA) and styryldehydroalanine (SDA) were synthesized and used as sensitive spectroscopic probes to study the acylation of papain by specific substrates and inhibitors. The spectral changes observed upon acylation of the enzyme with peptides containing these amino acids are large red shifts of the absorption maxima (lambda max) of the chromophores. The magnitudes of the absorption shifts were 49 nm (from 277 to 326 nm) for PDA peptide and 59 nm (from 318 to 377 nm) for SDA peptides. The following specific substrates were synthesized: Ac-Phe-Phe-PDA-OEt, Ac-Phe-PDA-NH2, Ala-Ala-Phe-SDA-OME, Ala-Ala-Phe-SDA-NH2, Lys-Ala-(o-benzyl)tyrosyl-SDA-OMe, and Lys-Ala-(o-benzyl)-tyrosyl-SDA-NH2. Similarly, the specific competitive inhibitors Ac-Phe-PDA (Ki = 5.3 X 10(-6) M), Z-Phe-SDA (Ki = 5.6 X 10(-5) M), Ala-Ala-Phe-SDA (Ki = 2.9 X 10(-5) M), and Lys-Ala-(o-benzyl)tyrosyl-SDA (Ki = 1.1 X 10(-5) M) were prepared. An additional chromophore was used to follow the noncovalent association of an inhibitor or substrate with papain, independently from the acylation or deacylation steps. This chromophore, which was introduced into the peptides at position P2, IS p-(p"-dimethylaminophenylazo) phenylalanine (DAP). The light absorption spectrum of DAP is dependent on its environment. The substrates Ala-Ala-DAP-SDA-OMe and Ala-Ala-DAP-SDA-NH2 and the competitive inhibitor Ala-Ala-DAP-SDA (Ki = 2.5 X 10(-6) M) were prepared. The noncovalent binding of these peptides to the active site of papain was followed either by the increase in the absorption at 480 nm or the decrease at 550 nm. With these petides the acylation and deacylation reactions could be followed simultaneously at 377 nm. The extent of acyl enzyme formation was found to decrease in a sigmoidal way with increasing pH, with a transition point around pH 5.5.
3. Flow Cytometry Reveals the Nature of Oncotic Cells
Anna Vossenkamper, Gary Warnes Int J Mol Sci. 2019 Sep 6;20(18):4379. doi: 10.3390/ijms20184379.
The term necrosis is commonly applied to cells that have died via a non-specific pathway or mechanism but strictly is the description of the degradation processes involved once the plasma membrane of the cell has lost integrity. The signalling pathways potentially involved in accidental cell death (ACD) or oncosis are under-studied. In this study, the flow cytometric analysis of the intracellular antigens involved in regulated cell death (RCD) revealed the phenotypic nature of cells undergoing oncosis or necrosis. Sodium azide induced oncosis but also classic apoptosis, which was blocked by zVAD (z-Vla-Ala-Asp(OMe)-fluoromethylketone). Oncotic cells were found to be viability+ve/caspase-3-ve/RIP3+ve/-ve (Receptor-interacting serine/threonine protein kinase 3). These two cell populations also displayed a DNA damage response (DDR) phenotype pH2AX+ve/PARP-ve, cleaved PARP induced caspase independent apoptosis H2AX-ve/PARP+ve and hyper-activation or parthanatos H2AX+ve/PARP+ve. Oncotic cells with phenotype cell viability+ve/RIP3-ve/caspase-3-ve showed increased DDR and parthanatos. Necrostatin-1 down-regulated DDR in oncotic cells and increased sodium azide induced apoptosis. This flow cytometric approach to cell death research highlights the link between ACD and the RCD processes of programmed apoptosis and necrosis.
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