Glycyl-L-tyrosine
[CAS# 658-79-7]

Identification

• Classification: Biochemical >> Amino acids and their derivatives >> Tyrosine derivatives
• Name: Glycyl-L-tyrosine
• Synonyms: N-Glycyl-L-tyrosine; Gly-Tyr
• Molecular Formula: C₁₁H₁₄N₂O₄
• Molecular Weight: 238.24
• Protein Sequence: GY
• CAS Registry Number: 658-79-7
• EC Number: 211-525-1
• SMILES: C1=CC(=CC=C1C[C@@H](C(=O)O)NC(=O)CN)O

Properties

• Density: 1.4±0.1 g/cm³ Calc.^*
• Melting point: 230 °°C)
• Boiling point: 568.4±50.0 °C 760 mmHg (Calc.)^*
• Flash point: 297.6±30.1 °C (Calc.)^*
• Index of refraction: 1.606 (Calc.)^*

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

Safety Data

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

Discovery and Applications

Glycyl-L-tyrosine is a dipeptide composed of two amino acids: glycine and L-tyrosine, linked by a single peptide bond. It is one of the simplest dipeptides, with the structure H₂NCH₂CONHCH(CH₂C₆H₄OH)COOH. This compound belongs to a broader class of bioactive peptides that are formed either through enzymatic digestion of proteins or by chemical synthesis for specific research and industrial applications.

Glycyl-L-tyrosine has been studied primarily as a model compound in biochemical and pharmaceutical research. The study of such small peptides provides important insights into peptide bond formation, stability, enzymatic hydrolysis, and transport mechanisms across biological membranes. The compound can be synthesized through standard peptide synthesis techniques, including solution-phase or solid-phase methods, and is used as a reference standard in analytical studies.

One of the important applications of glycyl-L-tyrosine is in the investigation of peptide transport systems, particularly the peptide transporter 1 (PEPT1) and peptide transporter 2 (PEPT2), which are responsible for the uptake of di- and tripeptides across cell membranes in the intestine and kidney. These transporters play a critical role in nutrient absorption and drug delivery, and glycyl-L-tyrosine serves as a substrate to evaluate their function and kinetics in in vitro and in vivo systems.

In pharmaceutical formulation, glycyl-L-tyrosine and related dipeptides are studied for their potential in prodrug strategies. By linking an active drug molecule to a dipeptide moiety such as glycyl-L-tyrosine, it is possible to enhance drug solubility, stability, or bioavailability. The dipeptide component may facilitate targeted delivery through peptide transporters, thereby improving the therapeutic profile of certain drugs.

Glycyl-L-tyrosine is also relevant in nutritional science, where dipeptides are evaluated for their digestibility and bioavailability. In protein hydrolysates and specialized nutritional formulations, dipeptides like glycyl-L-tyrosine are absorbed more efficiently than free amino acids or larger peptides. Their presence in dietary supplements, especially those designed for clinical nutrition, reflects their utility in conditions where rapid absorption of amino acids is needed.

In biochemical research, glycyl-L-tyrosine is used as a substrate in enzymatic studies to assess the activity of peptidases and proteases. These enzymes catalyze the cleavage of peptide bonds, and the rate of hydrolysis of glycyl-L-tyrosine can provide information about enzyme specificity and mechanism. It is also used in studies on the thermal and pH stability of peptide bonds, contributing to the understanding of peptide behavior under physiological and industrial processing conditions.

Analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and nuclear magnetic resonance (NMR) spectroscopy have employed glycyl-L-tyrosine as a reference or model compound for method development and validation. Its well-defined structure and physicochemical properties make it suitable for such purposes in both research and industrial laboratories.

In summary, glycyl-L-tyrosine is a dipeptide formed from glycine and L-tyrosine, widely used as a model compound in biochemistry, pharmaceutical research, nutritional science, and analytical chemistry. Its applications include studies of peptide transport, enzyme activity, drug delivery strategies, and protein hydrolysates, reflecting its versatility and significance in both scientific and applied contexts.

References

1906. Spaltung einiger Dipeptide durch Pankreasferment. Untersuchungen über Aminosäuren, Polypeptide und Proteïne (1899-1906), 1.
DOI: 10.1007/978-3-642-99499-9_41

2023. Standard Enthalpies of Formation of Glycyl-L-tyrosine and Its Dissociation Products in Aqueous Solutions. Russian Journal of Physical Chemistry A, 97(11).
DOI: 10.1134/s0036024423110171

2024. Exploring metabolic effects of dipeptide feed media on CHO cell cultures by in silico model-guided flux analysis. Applied Microbiology and Biotechnology, 108(1).
DOI: 10.1007/s00253-023-12997-0