N2-acetyl-L-arginyl-L-lysyl-L-alpha-aspartyl-L-valyl-L-tyrosine
[CAS# 97530-32-0]

Identification

• Classification: Biochemical >> Peptide
• Name: N2-acetyl-L-arginyl-L-lysyl-L-alpha-aspartyl-L-valyl-L-tyrosine
• Synonyms: (3S)-3-[[(2S)-2-[[(2S)-2-acetamido-5-(diaminomethylideneamino)pentanoyl]amino]-6-aminohexanoyl]amino]-4-[[(2S)-1-[[(1S)-1-carboxy-2-(4-hydroxyphenyl)ethyl]amino]-3-methyl-1-oxobutan-2-yl]amino]-4-oxobutanoic acid
• Molecular Formula: C₃₂H₅₁N₉O₁₀
• Molecular Weight: 721.80
• CAS Registry Number: 97530-32-0
• SMILES: CC(C)[C@@H](C(=O)N[C@@H](CC1=CC=C(C=C1)O)C(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCN=C(N)N)NC(=O)C

Properties

• Density: 1.4±0.1 g/cm³, Calc.^*
• Index of Refraction: 1.627, Calc.^*

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

Safety Data

• Hazard Symbols: GHS07 Warning
• Hazard Statements: H302-H315-H319-H335
• Precautionary Statements: P280-P305+P351+P338

Discovory and Applicatios

N2-acetyl-L-arginyl-L-lysyl-L-alpha-aspartyl-L-valyl-L-tyrosine is a synthetic pentapeptide featuring five amino acid residues with defined stereochemistry and an N-terminal acetyl modification. The sequence contains arginine and lysine, which are positively charged at physiological pH, aspartic acid, a negatively charged residue, valine, a hydrophobic residue, and tyrosine, which bears a phenolic group capable of hydrogen bonding and aromatic interactions. The N-terminal acetylation stabilizes the peptide by protecting it from exopeptidase degradation and mimics naturally occurring acetylated peptides, thereby facilitating experimental studies under physiological conditions.

The development of N2-acetyl-L-arginyl-L-lysyl-L-alpha-aspartyl-L-valyl-L-tyrosine reflects the maturation of solid-phase peptide synthesis methods, which allow sequential addition of protected amino acids to form peptides with precise sequence control. This peptide, like other small synthetic peptides, is valuable as a model compound to study enzymatic specificity, peptide–protein interactions, and structural effects of sequence variations. The inclusion of both basic and acidic residues allows investigation into electrostatic interactions, while hydrophobic and aromatic residues contribute to conformational stability and potential membrane association.

Structurally, the peptide displays amphiphilic characteristics. The positively charged arginine and lysine residues facilitate interactions with negatively charged biomolecules, such as nucleic acids or membrane phospholipids. Aspartic acid introduces a negative charge and hydrogen-bonding potential, valine contributes to hydrophobic interactions, and tyrosine’s hydroxyl group provides opportunities for hydrogen bonding or post-synthetic modifications. These features make the peptide suitable for mechanistic studies in enzymology, receptor-binding assays, and investigations of peptide-mediated signaling.

Applications of N2-acetyl-L-arginyl-L-lysyl-L-alpha-aspartyl-L-valyl-L-tyrosine are primarily research-oriented. In enzymology, it can be used to examine protease recognition and cleavage specificity, comparing the effects of acetylation and amino acid composition on susceptibility to enzymatic hydrolysis. The peptide also serves as a model for studying peptide–receptor interactions or ligand binding in cellular assays. Its combination of hydrophobic, basic, and acidic residues allows detailed exploration of sequence-dependent activity in biochemical and biophysical systems.

In analytical chemistry, this pentapeptide can act as a standard for chromatography and mass spectrometry. Its well-defined mass, sequence, and chemical stability facilitate accurate quantification and structural characterization. Additionally, the acetylation of the N-terminus and the presence of tyrosine provide chemical handles that may be used in derivatization or labeling experiments, further enhancing its utility as a research tool.

Although the peptide is not itself a therapeutic agent, its design exemplifies the broader use of synthetic peptides in biochemical research. By manipulating amino acid sequences and terminal modifications, scientists can probe structure–function relationships, study enzymatic behavior, and explore molecular recognition mechanisms in controlled systems.

Overall, N2-acetyl-L-arginyl-L-lysyl-L-alpha-aspartyl-L-valyl-L-tyrosine is a chemically defined pentapeptide engineered for research applications in peptide chemistry and molecular biology. Its combination of basic, acidic, hydrophobic, and aromatic residues, along with N-terminal acetylation, provides a versatile model for studying enzyme specificity, peptide interactions, and analytical characterization, illustrating the power of synthetic peptides as tools for investigating biochemical processes.