L-Lysyl-L-prolyl-L-valine
[CAS# 67727-97-3]

Identification

• Classification: Biochemical >> Peptide
• Name: L-Lysyl-L-prolyl-L-valine
• Synonyms: a-MSH (11-13); (2S)-2-[[(2S)-1-[(2S)-2,6-diaminohexanoyl]pyrrolidine-2-carbonyl]amino]-3-methylbutanoic acid
• Protein Sequence: KPV
• Molecular Formula: C₁₆H₃₀N₄O₄
• Molecular Weight: 342.43
• CAS Registry Number: 67727-97-3
• SMILES: CC(C)[C@@H](C(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCCN)N

Safety Data

• Hazard Symbols: GHS07 Warning
• Hazard Statements: H302-H315-H319
• Precautionary Statements: P501-P270-P264-P280-P302+P352-P337+P313-P305+P351+P338-P362+P364-P332+P313-P301+P312+P330

Discovory and Applicatios

L-Lysyl-L-prolyl-L-valine is a short synthetic tripeptide composed of the naturally occurring amino acids L-lysine, L-proline, and L-valine linked by peptide bonds. Compounds of this type emerged from the broader development of peptide chemistry in the twentieth century, when advances in amino acid isolation, peptide bond formation, and analytical techniques made it possible to prepare and study defined oligopeptides. Early work on small peptides was closely connected to efforts to understand protein structure and function, as peptides provided simplified models for investigating how amino acid sequence influences chemical and biological properties.

The systematic synthesis of short peptides such as L-Lysyl-L-prolyl-L-valine became practical after the introduction of protecting group strategies and stepwise coupling methods. The development of carbodiimide-mediated coupling and, later, solid-phase peptide synthesis allowed researchers to assemble peptides with controlled stereochemistry and sequence. These methodological advances enabled the routine preparation of tripeptides for biochemical research, standards, and intermediate use in more complex peptide and protein syntheses. L-Lysyl-L-prolyl-L-valine belongs to this class of well-defined oligopeptides that can be prepared reproducibly and characterized by established spectroscopic and chromatographic techniques.

From a structural perspective, the peptide incorporates functional features typical of biologically relevant sequences. The lysine residue contributes a basic side chain capable of protonation and ionic interactions, while proline introduces conformational constraints due to its cyclic structure. Valine provides a hydrophobic component that can influence folding tendencies and intermolecular interactions. Together, these residues form a compact tripeptide that reflects common motifs found in larger peptides and proteins. Because of this, L-Lysyl-L-prolyl-L-valine has value as a reference compound for studying peptide behavior, including solubility, charge properties, and interactions with enzymes or receptors under controlled conditions.

The applications of L-Lysyl-L-prolyl-L-valine are primarily in scientific research rather than direct therapeutic use. Small peptides are frequently employed as analytical standards in chromatography and mass spectrometry, where known sequences are used to calibrate instruments and validate methods for peptide identification. In biochemical research, defined tripeptides can serve as substrates or inhibitors in enzymatic assays designed to probe protease specificity or peptide transport mechanisms. The presence of lysine and proline residues makes L-Lysyl-L-prolyl-L-valine particularly relevant in studies of proteolytic enzymes that recognize basic or conformationally restricted sequences.

In addition, peptides of this size are often used as intermediates or building blocks in the synthesis of longer peptides. By incorporating a preassembled tripeptide segment, researchers can streamline the construction of more complex sequences while maintaining control over stereochemistry and sequence fidelity. L-Lysyl-L-prolyl-L-valine can thus function as a modular unit in peptide synthesis workflows, especially in laboratories focused on peptide hormones, signaling molecules, or structure–function studies of proteins.

Beyond synthetic and analytical uses, short peptides also play a role in fundamental studies of peptide–membrane interactions, transport across biological barriers, and stability under physiological conditions. While L-Lysyl-L-prolyl-L-valine itself is not associated with a specific endogenous biological function, its composition reflects motifs commonly encountered in natural peptides. This makes it useful for comparative studies aimed at understanding how sequence and residue composition influence peptide behavior in aqueous and biological environments.

Overall, L-Lysyl-L-prolyl-L-valine represents a well-defined synthetic tripeptide that illustrates the maturation of peptide chemistry from methodological innovation to routine application. Its significance lies not in a single unique biological activity, but in its utility as a research compound that supports analytical chemistry, enzymology, and peptide synthesis. Through such applications, it contributes to the broader scientific effort to understand and manipulate peptide and protein systems.

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