Glycyl-L-valyl-L-seryl-L-tryptophylglycyl-L-leucyl-L-arginine
[CAS# 1801959-12-5]

Identification

• Classification: Biochemical >> Peptide
• Name: Glycyl-L-valyl-L-seryl-L-tryptophylglycyl-L-leucyl-L-arginine
• Synonyms: PE 22-28; (2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[(2-aminoacetyl)amino]-3-methylbutanoyl]amino]-3-hydroxypropanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]acetyl]amino]-4-methylpentanoyl]amino]-5-(diaminomethylideneamino)pentanoic acid
• Protein Sequence: GVSWGLR
• Molecular Formula: C₃₅H₅₅N₁₁O₉
• Molecular Weight: 773.88
• CAS Registry Number: 1801959-12-5
• SMILES: CC(C)C[C@@H](C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)NC(=O)CNC(=O)[C@H](CC1=CNC2=CC=CC=C21)NC(=O)[C@H](CO)NC(=O)[C@H](C(C)C)NC(=O)CN

Properties

• Density: 1.4±0.1 g/cm³ Calc.^*
• Index of refraction: 1.65 (Calc.)^*

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

Discovory and Applicatios

Glycyl-L-valyl-L-seryl-L-tryptophylglycyl-L-leucyl-L-arginine is a short linear peptide composed of eight amino acid residues arranged in a defined sequence. Compounds of this type emerged from the development of modern peptide chemistry in the mid twentieth century, when advances in amino acid protection strategies and coupling reactions made it possible to prepare peptides with precise sequences in the laboratory. The decisive breakthrough for routine access to such molecules was the introduction of solid-phase peptide synthesis by Bruce Merrifield in the early 1960s. This method allowed peptides containing multiple residues, including those with bulky or reactive side chains such as tryptophan and arginine, to be assembled efficiently and reproducibly. The synthesis of defined oligopeptides such as glycyl-L-valyl-L-seryl-L-tryptophylglycyl-L-leucyl-L-arginine relies on these established principles and does not occur naturally unless explicitly identified as part of a larger protein.

The discovery of peptides of this length is therefore inseparable from the broader history of peptide synthesis rather than from the isolation of a specific natural product. As peptide chemistry matured, researchers began to design and prepare short sequences to probe the relationship between amino acid order and biological function. Synthetic peptides were used as simplified models of protein regions, enzyme substrates, receptor ligands, or antigenic determinants. The ability to include polar residues such as serine, hydrophobic residues such as valine and leucine, aromatic residues such as tryptophan, and basic residues such as arginine within a single sequence enabled systematic exploration of structure–activity relationships.

In practical terms, glycyl-L-valyl-L-seryl-L-tryptophylglycyl-L-leucyl-L-arginine belongs to a class of research peptides that are typically prepared as analytical standards or experimental tools. Such peptides have been employed in enzymology to study protease specificity, since defined sequences can be designed to contain potential cleavage sites and monitored for hydrolysis. They have also been used in receptor binding and signaling studies, where short peptides may mimic segments of endogenous proteins and interact with biological targets in a controlled manner. In immunological research, synthetic peptides of comparable length are frequently used as antigens to map epitopes recognized by antibodies or T cells, because they represent discrete, well-defined fragments of larger proteins.

Another important application of short synthetic peptides lies in analytical chemistry and biochemistry. Peptides like this one are commonly used as calibration or reference compounds in chromatographic and mass spectrometric methods. Their known composition and sequence allow validation of analytical performance, optimization of separation conditions, and confirmation of fragmentation patterns. The inclusion of tryptophan provides a convenient chromophore for ultraviolet detection, while the presence of arginine enhances ionization efficiency in mass spectrometry, making such peptides particularly useful in method development.

In more recent decades, designed oligopeptides have also been explored as building blocks in biomaterials science and chemical biology. Although glycyl-L-valyl-L-seryl-L-tryptophylglycyl-L-leucyl-L-arginine itself is not a commercial drug or established therapeutic agent, peptides of similar length and composition have been investigated for antimicrobial activity, cell-penetrating properties, or as components of peptide-based delivery systems. These studies build on the fundamental understanding gained from earlier peptide synthesis and characterization work, demonstrating how synthetic peptides can be tailored for specific experimental purposes.

Overall, the significance of glycyl-L-valyl-L-seryl-L-tryptophylglycyl-L-leucyl-L-arginine lies in its role as a representative synthetic peptide made possible by advances in peptide chemistry. Its discovery is rooted in methodological innovation rather than natural product isolation, and its applications are primarily in research settings where well-defined peptide sequences are required to investigate biochemical, analytical, or biological questions.

References

Merrifield RB (1963) Solid phase peptide synthesis. I. The synthesis of a tetrapeptide. Journal of the American Chemical Society 85 14 2149–2154 DOI: 10.1021/ja00897a025

Fields GB, Noble RL (1990) Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. International Journal of Peptide and Protein Research 35 3 161–214 DOI: 10.1111/j.1399-3011.1990.tb00939.x

Srinivasan R, Rose GD (1999) A physical basis for protein secondary structure. Proceedings of the National Academy of Sciences of the United States of America 96 25 14258–14263 DOI: 10.1073/pnas.96.25.14258