Ile-Met integrates hydrophobic isoleucine with sulfur-containing methionine, supporting oxidation studies and hydrophobic packing analysis. The peptide aids investigation of electron-donating side chains and conformational shifts. Researchers evaluate its folding behavior under varied conditions. Uses include redox modeling, motif exploration, and enzymatic-interaction studies.
CAT No: R2667
CAS No:42384-14-5
Synonyms/Alias:Ile-Met;L-isoleucyl-L-methionine;42384-14-5;Isoleucyl-Methionine;L-Ile-L-Met;SCHEMBL2550265;CHEBI:74073;AKOS010406396;FI108078;Q27144386;(S)-2-((2S,3S)-2-amino-3-methylpentanamido)-4-(methylthio)butanoic acid;(2S)-2-[[(2S,3S)-2-amino-3-methylpentanoyl]amino]-4-methylsulfanylbutanoic acid;
Ile-Met, also known as isoleucyl-methionine, is a synthetic dipeptide composed of the amino acids isoleucine and methionine linked via a peptide bond. As a representative of the peptide compound category, Ile-Met serves as a valuable tool in biochemical and molecular biology research due to its defined structure and functional properties. The combination of a branched-chain amino acid and a sulfur-containing amino acid within a single molecule provides unique opportunities for investigating peptide behavior, enzymatic processing, and protein engineering. Its relevance extends to studies focused on peptide metabolism, substrate specificity, and the role of dipeptides in cellular systems.
Peptide transport studies: Ile-Met is frequently utilized as a model substrate in research exploring peptide transport mechanisms across biological membranes. Its defined dipeptide structure makes it suitable for probing the specificity and kinetics of oligopeptide transporters, such as those in the SLC15 family. By tracking the uptake and movement of this dipeptide in cell-based or vesicular systems, researchers can better understand how small peptides are recognized and translocated, providing insights into nutrient absorption and pharmacokinetics at the cellular level.
Enzymatic hydrolysis assays: The dipeptide is widely employed in assays designed to characterize the activity and substrate preferences of peptidases and proteases. Its use enables the assessment of enzyme specificity, catalytic efficiency, and reaction mechanisms, especially for enzymes that target isoleucine- or methionine-containing peptide bonds. Results from such studies contribute to a deeper understanding of proteolytic pathways, enzyme regulation, and the development of selective inhibitors or activators for biochemical research.
Peptide synthesis validation: Ile-Met serves as a reference standard and validation substrate in the development and optimization of solid-phase peptide synthesis protocols. Its incorporation into synthetic workflows allows chemists to evaluate coupling efficiency, side-chain protection strategies, and the fidelity of peptide bond formation. Analytical assessment of the synthesized dipeptide supports method development for producing more complex peptides and proteins with precise sequence control.
Protein engineering and structural studies: The presence of both hydrophobic and sulfur-containing side chains in Ile-Met makes it a useful building block in protein engineering applications. Incorporating this dipeptide into recombinant proteins or peptide libraries facilitates the investigation of sequence-dependent folding, stability, and functional properties. Such studies are essential for elucidating structure-activity relationships and for the rational design of biomolecules with tailored characteristics.
Nutritional and metabolic research: In studies focused on amino acid metabolism and nutrient utilization, Ile-Met provides a controlled means to examine how dipeptides are processed compared to free amino acids. Its use in cell culture or animal models enables researchers to investigate absorption dynamics, metabolic fate, and the role of dipeptides in supporting cellular growth and function. Findings from these experiments inform our understanding of peptide-based nutrition and the physiological relevance of dipeptide transport and metabolism.
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