L-Aspartyl-L-phenylalanine is a dipeptide inhibitor of angiotensin-converting enzyme (ACE) and a metabolite of the synthetic non-caloric sweetener aspartame. It is formed from aspartame by intestinal intracellular esterases. L-Aspartyl-L-phenylalanine inhibits ACE with a Ki value of 11 µM for the rabbit enzyme. Serum levels of L-aspartyl-L-phenylalanine are positively associated with pancreatic ductal adenocarcinoma.
CAT No: 10-101-305
CAS No:13433-09-5
Synonyms/Alias:L-Aspartyl-L-phenylalanine;13433-09-5;H-ASP-PHE-OH;ASP-PHE;Aspartyl-phenylalanine;Aspartylphenylalanine;Demethylaspartame;l-a-aspartyl-l-phenylalanine;CHEBI:73830;L-alpha-Aspartyl-L-phenylalanine;(S)-3-Amino-4-(((S)-1-carboxy-2-phenylethyl)amino)-4-oxobutanoic acid;a-Aspartylphenylalanine;alpha-L-Aspartyl-L-phenylalanine;EINECS 236-557-3;(3S)-3-amino-4-[[(1S)-1-carboxy-2-phenylethyl]amino]-4-oxobutanoic acid;a-L-Aspartyl-L-phenylalanine;N-L-aspartyl-L-PhenylAlanine;CHEMBL170376;N-L-a-aspartyl-L-PhenylAlanine;N-L-alpha-aspartyl-L-PhenylAlanine;alpha-Aspartylphenylalanine;3-amino-N-(carboxyphenethyl)-Succinamic acid stereoisomer;3.Aspartame acid;3-amino-N-(a-carboxyphenethyl)-Succinamic acid stereoisomer;(S)-3-amino-4-((S)-1-carboxy-2-phenylethylamino)-4-oxobutanoic acid;MFCD00063155;.alpha.L-Aspartyl-L-phenylalanine;DF dipeptide;(3S)-3-amino-4-(((1S)-1-carboxy-2-phenylethyl)amino)-4-oxobutanoic acid;L-Aspartyl-L-phenylalanine; Aspartame Imp. B (EP); Aspartame Impurity B;alpha-Asp-Phe;D-F Dipeptide;L-a-Asp-L-phe;L-alpha-Asp-L-Phe;L-Asp-L-Phe;N-L-alpha-Aspartyl-3-phenyl-L-alanine;N-Aspartylphenylalanine;Asp-Phe, 96%;N-alpha-Aspartylphenylalanine;SCHEMBL135366;alphaL-Aspartyl-L-phenylalanine;N-L-alpha-Aspartylphenylalanine;Aspartate Phenylalanine dipeptide;Aspartate-Phenylalanine dipeptide;DTXSID20928570;YZQCXOFQZKCETR-UWVGGRQHSA-N;n-alpha-l-aspartyl-l-phenylalanine;13433-09-5 (free amine);Aspartic acid phenylalanine dipeptide;Aspartic acid-phenylalanine dipeptide;BDBM50049759;MSK001019;AKOS022180930;AS-46818;FA108005;1ST001019;CS-0044366;NS00014795;L-alpha-Aspartyl-L-phenylalanine Hydrochloride;F10617;N-L-alpha-Aspartyl-L-phenylalanine Hydrochloride;Q27144148;
Chemical Name:(3S)-3-amino-4-[[(1S)-1-carboxy-2-phenylethyl]amino]-4-oxobutanoic acid
Aspartyl-Phenylalanine (Asp-Phe) is a dipeptide composed of aspartic acid and phenylalanine, recognized for its versatile biochemical properties and significance in various research and industrial contexts. This compound is frequently employed in peptide synthesis and structural studies due to its well-defined amide bond and side-chain functionalities. The presence of both acidic and aromatic residues in Asp-Phe enables unique interactions with enzymes, receptors, and other biomolecules, making it a valuable tool in the exploration of protein-ligand interactions, substrate specificity, and conformational dynamics. Researchers appreciate its solubility characteristics and stability under a range of experimental conditions, which facilitate its integration into broader peptide libraries or as a model compound in analytical and preparative methodologies. The adaptability of Asp-Phe to diverse experimental needs underscores its importance within the fields of biochemistry, molecular biology, and materials science.
Peptide Synthesis Research: Asp-Phe is widely utilized as a building block in solid-phase and solution-phase peptide synthesis, allowing scientists to construct longer peptide chains with precise sequence control. Its incorporation into synthetic peptides enables the study of sequence-dependent folding, stability, and bioactivity, serving as a model system for understanding the influence of aspartic acid and phenylalanine residues on peptide conformation. Researchers often employ this dipeptide to optimize synthetic protocols, evaluate coupling reagents, and troubleshoot synthesis challenges, thereby advancing the development of novel peptide-based materials and therapeutics.
Enzyme Substrate Specificity Studies: In enzymology, Aspartyl-Phenylalanine serves as a substrate or reference standard for investigating protease and peptidase specificity. By monitoring the cleavage or modification of this dipeptide, scientists can elucidate the catalytic preferences of various enzymes, map active sites, and probe the mechanisms underlying peptide bond hydrolysis. Its defined structure and susceptibility to enzymatic action make it an ideal candidate for kinetic assays, inhibitor screening, and comparative studies across different enzyme families.
Protein-Ligand Interaction Analysis: The aromatic and acidic side chains of Asp-Phe facilitate its use in probing protein-ligand interactions, particularly in studies focused on binding affinity, recognition motifs, and allosteric modulation. Researchers utilize it as a ligand or competitive inhibitor in binding assays, surface plasmon resonance experiments, and nuclear magnetic resonance (NMR) spectroscopy. Such investigations help clarify the molecular determinants of specificity and affinity in protein-peptide complexes, contributing to advances in drug discovery, structural biology, and rational design.
Analytical Method Development: Asp-Phe is often employed as a standard or reference compound in chromatographic and spectroscopic method development. Its well-characterized physicochemical properties, including UV absorbance and chromatographic behavior, make it suitable for calibrating instruments, validating separation techniques, and quantifying peptide content in complex mixtures. Analytical chemists rely on it to assess method sensitivity, reproducibility, and robustness, ensuring accurate and reliable results in peptide analysis workflows.
Material Science and Functional Biomaterials: In the realm of materials science, Aspartyl-Phenylalanine is explored for its potential to self-assemble into nanostructures or serve as a functional motif in bio-inspired materials. Its amphiphilic nature and propensity for hydrogen bonding and π-π interactions enable the formation of ordered aggregates, hydrogels, or surface coatings with tunable mechanical and biochemical properties. Researchers investigate these assemblies for applications in tissue engineering, drug delivery, and biosensing, leveraging the unique chemical features of Asp-Phe to design advanced functional materials that mimic or enhance biological processes.
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