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Application Area

Acetyl-L-alanine methyl ester

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

L-Amino Acids

Catalog number

BAT-003863

CAS number

3619-02-1

Molecular Formula

C6H11NO3

Molecular Weight

145.16

IUPAC Name

methyl (2S)-2-acetamidopropanoate

Synonyms

Acetyl-L-alanine methyl ester; (S)-Methyl 2-acetamidopropanoate

Appearance

Yellow liquid

Purity

≥ 98% (HPLC)

Density

1.1088 g/cm3

Storage

Store at 2-8 °C

InChI

InChI=1S/C6H11NO3/c1-4(6(9)10-3)7-5(2)8/h4H,1-3H3,(H,7,8)/t4-/m0/s1

InChI Key

FQGVVDYNRHNTCK-BYPYZUCNSA-N

Canonical SMILES

CC(C(=O)OC)NC(=O)C

Acetyl-L-alanine methyl ester is a versatile compound with significant applications in the pharmaceutical industry. One of its key roles is as an intermediate in the synthesis of various amino acid derivatives and peptides. These derivatives are often used in the development of novel therapeutic agents, offering potential treatments for a range of medical conditions, including metabolic disorders, cardiovascular diseases, and cancer. By serving as a building block in the design of these bioactive molecules, Acetyl-L-alanine methyl ester contributes to the advancement of drug discovery and development, ultimately aiding in the creation of more effective and targeted treatments.

In the realm of biochemical research, Acetyl-L-alanine methyl ester is utilized as a substrate for studying enzyme specificity and activity. Researchers employ this ester in assays to understand the mechanisms of various enzymes, especially proteases, which play critical roles in many physiological processes. By providing a means to study enzyme interactions and kinetics, Acetyl-L-alanine methyl ester aids scientists in deciphering the complex biochemical pathways that regulate cell function and metabolism. This knowledge is crucial for the development of enzyme inhibitors or activators, which can be used as research tools or as potential therapeutic agents.

Another significant application of Acetyl-L-alanine methyl ester is in the field of agricultural sciences, particularly in the development of plant growth regulators and pesticides. The compound's structural properties allow for its integration into molecules that can influence plant physiology, such as enhancing growth rates, improving resistance to stress, and increasing crop yields. Moreover, its role in the formulation of new pesticides assists in protecting crops from pests more efficiently while potentially reducing the environmental impact compared to traditional chemical pesticides. This contribution is vital for sustainable agricultural practices and food security.

In the domain of material sciences, Acetyl-L-alanine methyl ester is explored for its potential in creating biodegradable polymers. These eco-friendly polymers are increasingly important as the world shifts towards sustainable materials to reduce environmental pollution. Acetyl-L-alanine methyl ester's incorporation into polymer chains can enhance the biodegradability of the material, making it suitable for applications such as packaging, disposable items, and medical devices, including sutures and drug delivery systems. The development of these polymers underscores the role of Acetyl-L-alanine methyl ester in advancing green chemistry and supporting the global effort to reduce plastic waste.

1. Binding Energies of Proton-Bound Dimers of Imidazole and n-Acetylalanine Methyl Ester Obtained by Blackbody Infrared Radiative Dissociation

R A Jockusch, E R Williams J Phys Chem A. 1998 Jun 11;102(24):4543-50. doi: 10.1021/jp980264w.

The dissociation kinetics of protonated n-acetyl-L-alanine methyl ester dimer (AcAlaME(d)), imidazole dimer, and their cross dimer were measured using blackbody infrared radiative dissociation (BIRD). Master equation modeling of these data was used to extract threshold dissociation energies (E(o)) for the dimers. Values of 1.18 +/- 0.06, 1.11 +/- 0.04, and 1.12 +/- 0.08 eV were obtained for AcAlaME(d), imidazole dimer, and the cross dimer, respectively. Assuming that the reverse activation barrier for dissociation of the ion-molecule complex is negligible, the value of E(o) can be compared to the dissociation enthalpy (DeltaH(d) degrees ) from HPMS data. The E(o) values obtained for the imidazole dimer and the cross dimer are in agreement with HPMS values; the value for AcAlaME(d) is somewhat lower. Radiative rate constants used in the master equation modeling were determined using transition dipole moments calculated at the semiempirical (AM1) level for all dimers and compared to ab initio (RHF/3-21G*) calculations where possible. To reproduce the experimentally measured dissociation rates using master equation modeling, it was necessary to multiply semiempirical transition dipole moments by a factor between 2 and 3. Values for transition dipole moments from the ab initio calculations could be used for two of the dimers but appear to be too low for AcAlaME(d). These results demonstrate that BIRD, in combination with master equation modeling, can be used to determine threshold dissociation energies for intermediate size ions that are in neither the truncated Boltzmann nor the rapid energy exchange limit.

2. Conformational properties of the residues connected by ester and methylated amide bonds: theoretical and solid state conformational studies

Dawid Siodłak, Anna Janicki J Pept Sci. 2010 Mar;16(3):126-35. doi: 10.1002/psc.1208.

Peptides produced by bacteria and fungi often contain an ester bond in the main chain. Some of them have both an ester and methylated amide bond at the same residue. A broad spectrum of biological activities makes these depsipeptides potential drug precursors. To investigate the conformational properties of such modified residues, a systematic theoretical analysis was performed on N-acetyl-L-alanine N'-methylamide (Ac-Ala-NHMe) and the analogues with the ester bond on the C-terminus (Ac-Ala-OMe), N-terminus (Ac-[psi](COO)-Ala-NHMe) as well as the analogues methylated on the N-terminus (Ac-(Me)Ala-OMe) and C-terminus (Ac-[psi](COO)-Ala-NMe(2)). The phi, psi potential energy surfaces and the conformers localised were calculated at the B3LYP/6-311++G(d,p) level of theory both in vacuo and with inclusion of the solvent (chloroform, water) effect (SCRF method). The solid state conformations of the studied residues drawn from The Cambridge Structural Database have been also analysed. The residues with a C-terminal ester bond prefer the conformations beta, C5, and alpha(R), whereas those with N-terminal ester bond prefer the conformations beta, alpha(R), and the unique conformation alpha' (phi, psi = -146 degrees , -12 degrees ). The residues with N-terminal methylated amide and a C-terminal ester bond prefer the conformations beta, beta2, and interestingly, the conformation alpha(L). The residues with a C-terminal methylated amide and an N-terminal ester bond adopt primarily the conformation beta. The description of the selective structural modifications, such as those above, is a step towards understanding the structure-activity relationship of the depsipeptides, limited by the structural complexity of these compounds.

3. Polydepsipeptides. 5. Experimental conformational analysis of poly(L-alanyl-L-lactic acid) and related model compounds

R T Ingwall, C Gilon, M Goodman Macromolecules. 1976 Sep-Oct;9(5):802-8. doi: 10.1021/ma60053a022.

In this paper we report an experimental conformational analysis of the depsipeptide model compounds acetyl-L-alanine methyl ester, acetyl-L-lactic acid N-methylamide, and acetyl-L-alanyl-L-lactic acid N-methylamide and of the sequential polydepsipeptide poly(L-alanyl-L-lactic acid). The model depsipeptides were examined in dilute organic solutions by infrared and nuclear magnetic resonance spectroscopy. Neither acetyl-L-alanine methyl ester nor acetyl-L-lactic acid N-methylamide assumes an intramolecularly hydrogen-bonded conformation. Acetyl-L-alanyl-L-lactic acid N-methylamide, on the other hand, in dilute chloroform or dilute carbon tetrachloride solutions, strongly favors a conformation with an intramolecular hydrogen bond between the N-H hydrogen atom of its N-methylamide group and the carbonyl oxygen atom of its acetyl group. Comparison of theoretical and experimental circular dichroism suggests that poly(L-alanyl-L-lactic acid) is partially ordered in chloroform solution with approximately 50% of its repeat units in the R10 helix, an ordered conformation found by our previous theoretical analysis to have a low intramolecular conformational energy.