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 Isoleucylmethionine or Isoleucine-Methionine dipeptide, is a synthetic dipeptide composed of the amino acids isoleucine and methionine. This compound is valued in biochemical research for its unique structure, which combines the hydrophobic, branched-chain properties of isoleucine with the sulfur-containing side chain of methionine. Its dual amino acid composition provides distinct physicochemical characteristics, making it a useful model for studying peptide bond formation, enzymatic cleavage, and peptide transport mechanisms. Researchers are increasingly utilizing Ile-Met in a range of laboratory settings to explore fundamental questions in protein chemistry and cellular metabolism.
Peptide Transport Studies: Ile-Met is frequently employed in the investigation of peptide transport systems, particularly those involving oligopeptide transporters in prokaryotic and eukaryotic cells. By tracing the uptake and intracellular fate of this dipeptide, scientists can gain insight into the specificity, kinetics, and regulatory mechanisms of peptide transporters. It serves as a model substrate to dissect the roles of various transporter proteins, helping to elucidate how cells acquire and utilize small peptides under different physiological conditions.
Protease Substrate Analysis: In enzymology, Isoleucylmethionine is utilized as a well-defined substrate for characterizing proteolytic enzymes. Its unique dipeptide bond and side chain functionalities allow for the detailed study of substrate specificity and catalytic efficiency among various proteases. By monitoring the cleavage of Ile-Met, researchers can identify enzyme preferences, optimize assay conditions, and discover potential inhibitors that modulate proteolytic activity. This application is particularly valuable in the development of biochemical assays for high-throughput screening.
Protein Engineering and Synthesis: The dipeptide is also instrumental in the field of protein engineering, where it is used to study peptide bond formation and stability. By incorporating Ile-Met into synthetic peptides or recombinant proteins, scientists can assess the impact of its sequence on protein folding, structural integrity, and functional properties. Its presence in engineered constructs enables the exploration of sequence-dependent effects on protein design, which is essential for advancing synthetic biology and biomaterials research.
Nutritional Biochemistry: In nutritional studies, Isoleucine-Methionine dipeptide is investigated for its role in amino acid absorption and metabolism. Researchers use it to model how dipeptides are digested, absorbed, and utilized in animal and cellular systems, providing valuable information on nutrient assimilation and metabolic regulation. This approach aids in understanding how dietary peptides contribute to overall amino acid availability and supports the development of optimized nutritional formulations for research purposes.
Peptide-Based Drug Design: Ile-Met finds application in drug discovery as a scaffold for designing peptide-based therapeutics. Its structural features make it a candidate for modifying peptide drugs to enhance stability, bioavailability, or target specificity. By integrating the dipeptide into lead compounds, medicinal chemists can systematically evaluate the effects of sequence variation on pharmacological properties, guiding the optimization of peptide drugs for research and preclinical studies.
Biophysical Characterization: In addition to its roles in biochemical and cellular studies, Isoleucylmethionine is used in the biophysical characterization of peptides and proteins. Researchers employ it in spectroscopic and chromatographic analyses to investigate peptide conformation, aggregation behavior, and interaction with biomolecules. These studies contribute to a deeper understanding of peptide structure-function relationships and facilitate the development of analytical methodologies for peptide research. Collectively, the diverse applications of Ile-Met underscore its importance as a versatile tool in modern biochemical and molecular biology research.
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