Alpha-Asp-Leu is a dipeptide that is the N-(L-alpha-aspartyl) derivative of L-leucine. It has a role as a human urinary metabolite. It derives from aspartic acid and leucine.
CAT No: 10-101-301
CAS No:3062-14-4
Synonyms/Alias:3062-14-4;H-Asp-Leu-OH;L-alpha-aspartyl-L-leucine;(S)-2-((S)-2-Amino-3-carboxypropanamido)-4-methylpentanoic acid;Asp-Leu;Aspartyl-Leucine;alpha-Asp-Leu;L-Aspartyl-L-Leucine;(2S)-2-[(2S)-2-AMINO-3-CARBOXYPROPANAMIDO]-4-METHYLPENTANOIC ACID;(2S)-2-[[(2S)-2-amino-3-carboxypropanoyl]amino]-4-methylpentanoic acid;?-asp-leu;MFCD00037286;L-alpha-Asp-L-Leu;N-L-|A-aspartyl-L-leucine;SCHEMBL3783635;CHEBI:68596;AKOS016004504;AS-57816;FA108001;CS-0154141;D81932;Q27137034;
Chemical Name:(2S)-2-[[(2S)-2-amino-3-carboxypropanoyl]amino]-4-methylpentanoic acid
Asp-Leu, also known as Aspartyl-Leucine or DL dipeptide, is a synthetic dipeptide composed of the amino acids aspartic acid and leucine linked via a peptide bond. This compound is highly valued in scientific research due to its ability to mimic naturally occurring peptide fragments and its versatility in biochemical studies. Asp-Leu exhibits unique physicochemical properties, including solubility in aqueous solutions and stability under various laboratory conditions, making it a reliable component for experimental protocols. Its structural simplicity, combined with the presence of both acidic and hydrophobic residues, allows it to participate in a wide range of molecular interactions, facilitating its use in diverse research applications. Researchers often select Asp-Leu for its role as a model peptide, enabling the exploration of peptide behavior, enzymatic hydrolysis, and structure-activity relationships in controlled settings.
Peptide Transport Mechanism Studies: Aspartyl-Leucine serves as an ideal substrate for investigating peptide transporters such as PEPT1 and PEPT2 in cellular and molecular biology research. By utilizing radiolabeled or fluorescently tagged Asp-Leu, scientists can monitor the uptake, translocation, and specificity of peptide transport systems in epithelial and other cell types. These studies provide critical insights into nutrient absorption, drug delivery mechanisms, and the pharmacokinetics of peptide-based therapeutics, helping to elucidate how dipeptides traverse biological membranes and interact with transport proteins.
Enzyme Substrate Specificity Research: Asp-Leu is frequently employed as a model substrate for examining the specificity and catalytic efficiency of various peptidases, including dipeptidyl peptidases and exopeptidases. By analyzing the hydrolysis of Aspartyl-Leucine under controlled enzymatic reactions, researchers can characterize enzyme kinetics, substrate preferences, and the effects of inhibitors or mutations on enzymatic activity. These findings contribute to a deeper understanding of protein digestion, metabolic regulation, and the development of enzyme-targeted inhibitors for research purposes.
Protein Engineering and Peptide Mapping: The dipeptide Asp-Leu plays a significant role in protein engineering, where it is used to introduce specific sequence motifs or to probe the effects of sequence alterations on protein structure and function. In peptide mapping experiments, Asp-Leu serves as a reference compound or internal standard, facilitating the identification and quantification of peptide fragments generated by proteolytic digestion. Its predictable behavior during chromatographic separation and mass spectrometric analysis enhances the accuracy and reproducibility of proteomic workflows, supporting advanced studies in protein characterization.
Cell Signaling Pathway Exploration: Aspartyl-Leucine is utilized in cell biology to investigate the influence of dipeptides on intracellular signaling cascades. By administering Asp-Leu to cultured cells, researchers can assess its impact on signal transduction pathways, gene expression, and cellular responses such as proliferation or differentiation. These experiments help delineate the role of small peptides as modulators of cellular communication and provide a foundation for exploring peptide-based regulators of biological processes.
Peptide Stability and Degradation Analysis: Asp-Leu is instrumental in studies focused on peptide stability, degradation pathways, and the identification of metabolic products. By subjecting the dipeptide to various physiological or experimental conditions, scientists can monitor its degradation kinetics, identify cleavage products, and evaluate the influence of environmental factors such as pH, temperature, or enzymatic activity. These investigations inform the design of more stable peptide analogs and contribute to the understanding of peptide turnover in biological systems, thereby supporting the advancement of peptide research and biotechnological innovation.
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