Ala-Ile pairs a small alanine residue with a hydrophobic isoleucine to analyze steric influences on backbone conformation. The dipeptide provides a simple system for studying β-sheet and helix-initiation tendencies. Researchers examine its hydrogen-bonding patterns and solvent interactions. Applications include folding simulations, enzymatic recognition studies, and peptide-assembly modeling.
CAT No: R2660
CAS No:29727-65-9
Synonyms/Alias:ALA-ILE;L-alanyl-L-isoleucine;H-Ala-Ile-OH;29727-65-9;alanylisoleucine;AI dipeptide;alanyl-isoleucine;A-I Dipeptide;CHEBI:73805;L-Isoleucine, L-alanyl-;Alanine Isoleucine dipeptide;Alanine-Isoleucine dipeptide;(2S,3S)-2-[[(2S)-2-aminopropanoyl]amino]-3-methylpentanoic acid;(2S,3S)-2-[(2S)-2-AMINOPROPANAMIDO]-3-METHYLPENTANOIC ACID;N-Alanylisoleucine;DTXSID00875836;(2S,3S)-2-(((2S)-2-aminopropanoyl)amino)-3-methylpentanoic acid;(2S,3S)-2-(((2S)-2-azaniumylpropanoyl)amino)-3-methylpentanoate;(2S,3S)-2-[[(2S)-2-azaniumylpropanoyl]amino]-3-methylpentanoate;MFCD00025552;L-Ala-L-Ile;N-L-Alanyl-L-isoleucine;SCHEMBL934499;CHEMBL1221665;ZSOICJZJSRWNHX-ACZMJKKPSA-N;DTXCID201013953;AKOS010419877;FA107966;Q27144121;(2S,3S)-2-((S)-2-Aminopropanamido)-3-methylpentanoic acid;
Ala-Ile, also known as Alanine-Isoleucine, is a dipeptide composed of the amino acids alanine and isoleucine linked by a peptide bond. This compound is characterized by its stability and solubility in aqueous environments, making it a versatile tool for various biochemical and research applications. As a synthetic peptide, Ala-Ile is frequently utilized in studies exploring peptide structure, enzymatic activity, and protein interactions. Its manageable size and defined sequence enable precise experimental control, allowing researchers to investigate fundamental biological processes and molecular mechanisms. Additionally, its compatibility with a wide range of analytical techniques, such as mass spectrometry and chromatography, further enhances its value in laboratory settings.
Peptide Structure-Activity Relationship Studies: Ala-Ile serves as a model dipeptide in structure-activity relationship (SAR) research, where scientists examine how specific amino acid sequences influence the biological activity of peptides. By incorporating Ala-Ile into peptide libraries or modifying existing sequences, researchers can systematically analyze the impact of side-chain properties and backbone conformations on binding affinity, enzymatic recognition, or receptor activation. This approach provides valuable insights into the design of novel bioactive peptides and the optimization of therapeutic candidates.
Protease Substrate Profiling: In enzymology, Alanine-Isoleucine is frequently used as a substrate or substrate analog for characterizing protease specificity and activity. By monitoring the hydrolysis of Ala-Ile-containing peptides, investigators can determine the substrate preferences of various proteolytic enzymes, facilitating the discovery of new inhibitors or the development of enzyme assays. The dipeptide's defined structure and predictable cleavage sites make it an ideal candidate for kinetic studies and mechanistic investigations in protease research.
Peptide Transport and Uptake Studies: The dipeptide Ala-Ile is instrumental in studies focused on peptide transporters and cellular uptake mechanisms. Researchers employ radiolabeled or fluorescently tagged forms of this compound to track its movement across biological membranes, elucidating the function and selectivity of peptide transport proteins. These experiments are essential for understanding nutrient absorption, drug delivery, and the pharmacokinetics of peptide-based therapeutics, as well as for screening transporter modulators in drug discovery programs.
Analytical Method Development: Alanine-Isoleucine is often utilized as a standard or calibration compound in the development of analytical methods for peptide quantification and characterization. Its well-defined structure and consistent behavior in chromatographic and spectrometric analyses make it suitable for validating assay sensitivity, accuracy, and reproducibility. Scientists leverage Ala-Ile to optimize sample preparation protocols, refine detection parameters, and ensure the reliability of analytical workflows in both research and industrial laboratories.
Biophysical and Computational Modeling: In the field of biophysics and computational chemistry, Ala-Ile provides a tractable system for modeling peptide folding, stability, and intermolecular interactions. Its simplicity allows for detailed molecular dynamics simulations and quantum mechanical calculations, which help elucidate the fundamental principles governing peptide behavior. These studies contribute to the broader understanding of protein folding, aggregation, and the physicochemical properties of peptide-based materials.
Peptide Library Construction: Researchers frequently incorporate Alanine-Isoleucine into combinatorial peptide libraries for high-throughput screening and functional analysis. By varying the position or context of Ala-Ile within longer peptide sequences, scientists can probe the effects of sequence diversity on biological activity, binding specificity, or structural properties. This application supports the discovery of new ligands, enzyme substrates, and functional motifs, advancing research in chemical biology, drug design, and synthetic peptide engineering.
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