N2-Acetyl-L-glutaminyl-L-alpha-aspartyl-L-valyl-L-histidine
[CAS# 928006-50-2]

Identification

• Classification: Biochemical >> Peptide
• Name: N2-Acetyl-L-glutaminyl-L-alpha-aspartyl-L-valyl-L-histidine
• Synonyms: (3S)-3-[[(2S)-2-acetamido-5-amino-5-oxopentanoyl]amino]-4-[[(2S)-1-[[(1S)-1-carboxy-2-(1H-imidazol-5-yl)ethyl]amino]-3-methyl-1-oxobutan-2-yl]amino]-4-oxobutanoic acid
• Protein Sequence: QDVH
• Molecular Formula: C₂₂H₃₃N₇O₉
• Molecular Weight: 539.54
• CAS Registry Number: 928006-50-2
• SMILES: CC(C)[C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(=O)N)NC(=O)C

Properties

• Solubility: Soluble (39 g/L) (25 ºC), Calc.^*
• Density: 1.383±0.06 g/cm³ (20 ºC 760 Torr), Calc.^*
• Boiling point: 1169.0±65.0 ºC 760 mmHg (Calc.)^*
• Flash point: 660.8±34.3 ºC (Calc.)^*
• Index of refraction: 1.57 (Calc.)^*

^* Calculated using Advanced Chemistry Development (ACD/Labs) Software.

Safety Data

• Hazard Symbols: GHS07 Warning
• Hazard Statements: H302-H315-H319-H335
• Precautionary Statements: P261-P305+P351+P338

Discovory and Applicatios

N2-Acetyl-L-glutaminyl-L-alpha-aspartyl-L-valyl-L-histidine is a synthetic pentapeptide composed of a defined sequence of amino acid residues, with an N-terminal acetyl group and free carboxyl termini. The peptide combines polar, acidic, and basic amino acids, including glutamine, aspartic acid, valine, and histidine, creating a molecule with distinct chemical and biological properties. Such peptides are designed for stability, precise structural characterization, and investigation of sequence-dependent biological activity.

The preparation of N2-acetyl-L-glutaminyl-L-alpha-aspartyl-L-valyl-L-histidine arises from advances in solid-phase peptide synthesis developed in the mid-twentieth century. Solid-phase methods enabled the sequential coupling of protected amino acids to build oligopeptides with high fidelity. The acetylation of the N-terminal glutamine was introduced to enhance stability against exopeptidases and to mimic naturally acetylated peptide motifs found in proteins and signaling peptides. These modifications are critical for maintaining peptide integrity in biological studies.

Chemically, the peptide exhibits properties influenced by its amino acid composition. Acidic residues like aspartic acid provide negative charge and hydrogen bonding capacity, while histidine contributes an imidazole side chain that can act as a proton donor or acceptor near physiological pH. Glutamine adds additional polar functionality, and valine introduces hydrophobic character, balancing solubility and structural rigidity. The combination of these features makes the peptide useful for studying interactions with enzymes, receptors, and metal ions, as well as for probing the influence of amino acid sequence on stability and conformation.

Applications of N2-acetyl-L-glutaminyl-L-alpha-aspartyl-L-valyl-L-histidine are primarily in biochemical and pharmacological research. It serves as a model compound for investigating enzymatic specificity, particularly in peptidases and proteases. By comparing the activity of enzymes toward acetylated versus non-acetylated peptides, researchers can explore mechanisms of substrate recognition and degradation. Additionally, the peptide can be employed in studies of receptor binding and signaling, where short sequences containing histidine and acidic residues often play key roles in ligand recognition.

The pentapeptide is also valuable in analytical chemistry as a standard for chromatographic and mass spectrometric methods. Its defined sequence, molecular weight, and stability allow precise calibration and validation of techniques for peptide quantification. Such standards are essential for evaluating peptide metabolism, degradation rates, and the efficiency of synthetic protocols.

In addition to experimental studies, peptides like N2-acetyl-L-glutaminyl-L-alpha-aspartyl-L-valyl-L-histidine provide insight into structure–activity relationships. Researchers can systematically modify individual residues or terminal groups to assess how these changes affect biochemical interactions. These studies have informed the rational design of peptide-based probes, enzyme inhibitors, and signaling analogs, contributing to broader understanding of peptide chemistry and biology.

While N2-acetyl-L-glutaminyl-L-alpha-aspartyl-L-valyl-L-histidine is not itself a therapeutic agent, its importance lies in research contexts where chemically defined peptides serve as tools to investigate fundamental biochemical processes. Its synthesis and use illustrate how precise chemical modification of short amino acid sequences enables controlled exploration of enzymatic behavior, molecular recognition, and structural effects.

Overall, N2-acetyl-L-glutaminyl-L-alpha-aspartyl-L-valyl-L-histidine exemplifies the application of modern peptide chemistry to biochemical research. Through careful design and synthesis, it functions as a stable, well-characterized model compound, facilitating studies of enzyme activity, receptor interactions, and analytical methods, and providing insights into the interplay between peptide structure and function.

References

2018. The Chemical and Products Database, a resource for exposure-relevant data on chemicals in consumer products. Scientific Data, 5.
DOI: 10.1038/sdata.2018.125