51513-59-8

Usage

Uses

Used in Peptide Synthesis:
L-Alanylglycine methyl ester serves as a fundamental building block in the synthesis of peptides, contributing to the formation of more complex organic molecules. Its role in this process is crucial for the development of novel peptide-based compounds.
Used in Pharmaceutical Development:
In the pharmaceutical industry, L-Alanylglycine methyl ester is utilized in the research and development of new drugs. Its properties allow it to be integrated into the molecular structures of potential therapeutic agents, enhancing their efficacy and pharmacological profiles.
Used in Protein and Peptide Structure Research:
L-Alanylglycine methyl ester is also employed in the study of protein and peptide structures. It aids researchers in understanding the fundamental building blocks of these biological macromolecules, which is essential for advancing knowledge in biochemistry and molecular biology.

InChI:InChI=1/C6H12N2O3/c1-4(7)6(10)8-3-5(9)11-2/h4H,3,7H2,1-2H3,(H,8,10)/t4-/m0/s1

Upstream product

• 7360-10-3 o-Nitro-phenylsulfenyl-Ala-Gly-OMe 
• 4840-29-3 Z-L-Ala-Gly-OMe 
• 26061-06-3 methyl 2-((2S)-2-((tert-butoxycarbonyl)amino)propanamido)acetate 

Downstream Products

• 86895-15-0 Boc-Cys(MBzl)-Ala-Gly-OMe 
• 103527-56-6 Z(OMe)-Ser(Bzl)-Ala-Gly-OMe 
• 95753-61-0 phenylthiocarbamoyl-L-alanylglycine methyl ester 
• 161007-35-8 Boc-Gly-Lys(Z)-Tyr(Bzl)-Ser(Bzl)-Ala-Gly-OCH₃ 
• 94989-55-6 DppPhe-Ala-GlyOMe 
• 4526-77-6 L-alanylglycine diketopiperazine 
• 62570-90-5 Boc-Tyr(Bzl)-Ala-Ala-Gly-OMe 
• 62570-91-6 Boc-Tyr(Bzl)-Ala-Ala-Gly 
• 62570-92-7 Tyr-Ala-Ala-Gly 
• 25198-71-4 Ala-Ala-Gly 
• 98477-85-1 Z(OMe)-Leu-Asn-Ser(Bzl)-Ala-Gly-NHNH₂ 

Relevant academic research and scientific papers

Tripeptide-induced modulation of mesenchymal stem cell biomechanics stimulates proliferation and wound healing

We demonstrate the ability of two tripeptides to promote proliferation and modulate the mechanical properties of human mesenchymal stem cells (hMSCs). Notably, Young's modulus of peptide-treated hMSCs was found to be ～2 fold higher compared to the control group. These peptides promoted wound healing in hMSCs, without stimulating osteogenic and adipogenic differentiation, thus showing high potential in vascular tissue engineering applications.

Investigation of permeation of theophylline through skin using selected piperazine-2,5-diones

Transdermal administration of drugs that penetrate, in this case directly into the blood circulation, has many advantages and is promising for many drugs thanks to its easy application and good patient compliance. (S)-8-Methyl-6,9-diazaspiro[4.5]decan-7,10-dione (alaptide), has been studied as a potential chemical permeation enhancer. Based on its structure, four selected piperazine-2,5-diones were synthesized by means of multi-step synthetic pathways. All the compounds were investigated on their ability to enhance the permeation of the model drug theophylline from the hydrophilic medium propylene glycol:water (1:1). In vitro experiments were performed using vertical Franz diffusion cells at constant temperature 34 ± 0.5 ?C and using full-thickness pig (Sus scrofa f. domestica) ear skin. Withdrawn samples were analyzed by RP-HPLC for determination of the permeated amount of theophylline. All the compounds were applied in ratio 1:10 (w/w) relative to the amount of theophylline. One hour after application, the permeated amount of theophylline from formulations with alaptide and (3S,6S)-3,6-dimethylpiperazine-2,5-dione, was ca. 15- and 12-fold higher, respectively, than from the formulation without the tested compounds. Despite the enhancement ratio of both enhancers in a steady state was ca. 2.3, the pseudo-enhancement ratio in the time range from 1 to 3 h was 4.4. These enhancement ratios indicate that the compounds are able to enhance the permeation of agents through the skin; however, the short-term application of both compound formulations seems to be more advantageous. In addition, the screening of the cytotoxicity of all the prepared compounds was performed using three cell lines, and the compounds did not show any significant toxic effect.

Engineered Substrate for Cyclooxygenase-2: A Pentapeptide Isoconformational to Arachidonic Acid for Managing Inflammation

Beyond the conventional mode of working of anti-inflammatory agents through enzyme inhibition, herein, COX-2 was provided with an alternate substrate. A proline-centered pentapeptide isoconformational to arachidonic acid, which exhibited appreciable selectivity for COX-2, overcoming acetic acid- and formalin-induced pain in rats to almost 80%, was treated as a substrate by the enzyme. Remarkably, COX-2 metabolized the pentapeptide into small fragments consisting mainly of di- and tripeptides that ensured the safe breakdown of the peptide under in vivo conditions. The kinetic parameter Kcat/Km for COX-2-mediated metabolism of the peptide (6.3 × 105 M-1 s-1) was quite similar to 9.5 × 105 M-1 s-1 for arachidonic acid. Evidenced by the molecular dynamic studies and the use of Y385F COX-2, it was observed that the breakage of the pentapeptide has probably been taken place through H-bond activation of the peptide bond by the side chains of Y385 and S530.

Cleavable Amide Bond: Mechanistic Insight into Cleavable 4-Aminopyrazolyloxy Acetamide at Low pH

The cleavage of amide bonds under mild acidic conditions is a rare chemical event. N-Acetamide bond of peptides is extremely stable even under the strongest organic acid trifluoromethanesulfonic acid. This report mechanistically describes a new cleavable amide bond in 4-aminopyrazolyloxy acetamide peptide analogues under mild acidic conditions such as trifluoroacetic acid (10-20%) or HCl (0.1-4.0 N) at room temperature, and the formation of unusual lactam from 4-aminopyrazolyloxy acetic acid after evaporation of solvent. This is a rare chemical event in peptide bond, which could be explored as acid-sensitive protecting group of free amines.

Cleavable Amide Bond: Mechanistic Insight into Cleavable 4-Aminopyrazolyloxy Acetamide at Low pH

The cleavage of amide bonds under mild acidic conditions is a rare chemical event. N-Acetamide bond of peptides is extremely stable even under the strongest organic acid trifluoromethanesulfonic acid. This report mechanistically describes a new cleavable amide bond in 4-aminopyrazolyloxy acetamide peptide analogues under mild acidic conditions such as trifluoroacetic acid (10-20%) or HCl (0.1-4.0 N) at room temperature, and the formation of unusual lactam from 4-aminopyrazolyloxy acetic acid after evaporation of solvent. This is a rare chemical event in peptide bond, which could be explored as acid-sensitive protecting group of free amines.

Synthesis and biological evaluation of novel FK228 analogues as potential isoform selective HDAC inhibitors

Novel C4- and C7-modified FK228 analogues were efficiently synthesized in a highly convergent and unified manner. This synthesis features the amide condensation of glycine-d-cysteine-containing segments with d-valine-containing segments for the direct assembly of the corresponding seco-acids, which are key precursors of macrolactones. The HDAC inhibition assay and cell-growth inhibition analysis of the synthesized analogues revealed novel aspects of their structure-activity relationship. This study demonstrated that simple modification at the C4 and C7 side chains in FK228 is effective for improving both HDAC inhibitory activity and isoform selectivity; moreover, potent and highly isoform-selective class I HDAC1 inhibitors were identified.

"Backdoor Induction" of chirality in asymmetric hydrogenation with rhodium(I) complexes of amino acid substituted triphenylphosphane ligands

This paper describes the synthesis and characterization of 5-(diphenylphosphanyl)isophthalic acid bioconjugates (Lig-[R]2). In addition to symmetrically disubstituted conjugates with amino acids, peptides or amines, a convenient one-pot, two-step procedure for the synthesis of conjugates bearing two different substituents is reported. The 28 prepared phosphanes were used as monodentate ligands in the rhodium(I)-catalyzed hydrogenation of 2-acetamidoacrylate and (Z)-α-acetamidocinnamate. The ligand with the smallest side-chain substituents Lig-[Ala-OMe]2 (1a) revealed the highest selectivity, with up to 84 % ee. The catalysts presented herein are models of artificial metalloenzymes in which the outer-coordination sphere controls the selectivity in catalysis. The chirality of distant hydrogen-bonded amino acids is transmitted by "backdoor induction" to the prochiral RhI center. Models of artificial metalloenzymes are presented in which the outer-coordination sphere controls the selectivity in catalysis. The chirality of distant hydrogen-bonded amino acids or amines is transmitted by "backdoor induction" to the prochiral RhI center. Copyright

SYNTHESIS OF FRAGMENTS OF THE VP1 PROTEIN OF TYPE A22 FOOT-AND-MOUTH DISEASE VIRUS. SYNTHESIS OF FRAGMENTS 134-139, 134-145, 140-145, 150-155, AND 150-159

Fragments of peptides of the amino acid sequences (134-145) and (150-159) of the VP1 protein of the type A22 foot-and-mouth disease (FMD)virus have been synthesized by the classical methods of peptide chemistry.Oligopeptides were obt

Amino Acids and Peptides. III. Synthesis of Model Peptides Related to Cytochrome P-450

Various tetra- and pentapeptides with Cys and Ser (Thr, Tyr, His) at the N- and C-terminals, respectively, were synthetized as model peptides of the apoprotein of cytochrome P-450.The optical spectra of synthetic peptide-hemin complexes were measured and the results are discussed.Keywords - cytochrome P-450; synthetic Cys-containing peptide; peptide-hemin complex; optical spectrum of peptide-hemin complex