3146-40-5

Usage

Uses

Used in Research Applications:
H-ALA-GLY-GLY-OH is used as a research tool for studying enzyme kinetics and protein-protein interactions due to its ability to mimic the biochemical properties of certain proteins and peptides in the body.
Used in Pharmaceutical Development:
H-ALA-GLY-GLY-OH is used as a substrate in the development of novel peptide-based drugs, leveraging its role in peptide metabolism and synthesis to create new therapeutic agents.
Used in Drug Delivery Systems:
While not explicitly mentioned in the provided materials, given its role as a substrate for enzymes and its potential in pharmaceutical development, H-ALA-GLY-GLY-OH could also be utilized in drug delivery systems to improve the efficacy and targeted delivery of peptide-based therapeutics.
Used in Enzyme Assays:
H-ALA-GLY-GLY-OH is used as a substrate in enzyme assays to evaluate the activity and specificity of enzymes involved in peptide metabolism, providing insights into their mechanisms of action and potential as therapeutic targets.
Used in Biochemical Education:
In educational settings, H-ALA-GLY-GLY-OH can serve as a model compound to illustrate the structure and function of peptides, as well as the principles of enzyme catalysis and substrate specificity.

InChI:InChI=1/C7H13N3O4/c1-4(8)7(14)10-2-5(11)9-3-6(12)13/h4H,2-3,8H2,1H3,(H,9,11)(H,10,14)(H,12,13)

Upstream product

• 21929-69-1 N-benzyloxycarbonyl-L-alanyl-glycyl-glycine 
• 29022-11-5 N-(fluoren-9-ylmethoxycarbonyl)glycine 
• 35661-39-3 N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 

Downstream Products

• 76927-13-4 N^α-Z-L-tryptophyl-L-alanyl-glycyl-glycine 

Relevant academic research and scientific papers

In Situ N-Phosphorylation of Oligopeptides for Fast Atom Bombardment Mass Spectrometry

Positive ion fast atom bombardment mass spectrometry (FABMS) of in situ N-phosphorylated oligopeptides showed intense quasi-molecular ions together with the successive alkene loss fragment ions, which afford multiple checks of the unequivocal reality of the relative molecular mass of the tested samples.More interesting, in a novel cleavage pattern only the N-phosphoryl fragment ions gave intense peaks, the C-terminal series ions being suppressed.For each of the N-terminal ions, losses of alkenes also occur to provide multiple checks for the existence of these ions.The FABMS of the in situ N-phosphorylated oligopeptides might provide an easily accessible routine method for peptide sequencing.

Determination of peptide backbone torsion angles using double-quantum dipolar recoupling solid-state NMR spectroscopy

Several approaches for utilizing dipolar recoupling solid-state NMR (ssNMR) techniques to determine local structure at high resolution in peptides and proteins have been developed. However, many of these techniques measure only one torsion angle or are accurate for only certain classes of secondary structure. Additionally, the efficiency with which these dipolar recoupling experiments suppress the deleterious effects of chemical shift anisotropy (CSA) at high magnetic field strengths varies. Dipolar recoupling with a windowless sequence (DRAWS) has proven to be an effective pulse sequence for exciting double-quantum (DQ) coherences between adjacent carbonyl carbons along the peptide backbone. By allowing this DQ coherence to evolve, it is possible to measure the relative orientations of the CSA tensors and subsequently use this information to determine the Ramachandran torsion angles φ and ψ. Here, we explore the accuracies of the assumptions made in interpreting DQ-DRAWS data and demonstrate their fidelity in measuring torsion angles corresponding to a variety of secondary structures irrespective of hydrogen-bonding patterns. It is shown how a simple choice of isotopic labels and experimental conditions allows accurate measurement of backbone secondary structures without any prior knowledge. This approach is considerably more sensitive for determining structure in helices and has comparable accuracy for β-sheet and extended conformations relative to other methods. We also illustrate the ability of DQ-DRAWS to distinguish between structures in heterogeneous samples.