D-Leucylglycylglycine combines a D-configured hydrophobic residue with two flexible glycines, enabling stereochemical and conformational analysis. The sequence helps dissect how D-residues alter backbone geometry and recognition by proteases. Researchers evaluate its folding behavior and stability in solution. Applications include chirality studies, peptidomimetic design, and enzyme-specificity profiling.
CAT No: R2369
CAS No:18625-22-4
Synonyms/Alias:18625-22-4;D-Leucylglycylglycine;(R)-2-(2-(2-Amino-4-methylpentanamido)acetamido)acetic acid;2-[[2-[[(2R)-2-amino-4-methylpentanoyl]amino]acetyl]amino]acetic acid;CHEMBL1222388;H-D-Leu-Gly-Gly-OH;2-[[2-[[(2R)-2-azaniumyl-4-methylpentanoyl]amino]acetyl]amino]acetate;D-Leucyl-glycyl-glycine;Glycine,D-leucylglycyl-;Glycine, N-(N-D-leucylglycyl)-;N-(N-D-Leucylglycyl)glycine;2-{2-[(2R)-2-Amino-4-methylpentanamido]acetamido}acetic acid;EINECS 242-457-0;D-LEU-GLY-GLY;(([(2-Amino-4-methylpentanoyl)amino]acetyl)amino)acetic acid #;{2-[(2R)-2-amino-4-methylpentanamido]acetamido}acetic acid;DTXSID601314917;(R)-2-(2-(2-Amino-4-methylpentanamido)-acetamido)acetic acid;TAA62522;BDBM50410267;AKOS015854090;NSC 523307;AS-70790;CS-0320767;L0031;NS00085542;A12180;(R)-2-(2-(2-Amino-4-methylpentanamido)acetamido)aceticacid;
D-Leucylglycylglycine is a synthetic tripeptide composed of D-leucine, glycine, and glycine residues arranged in a specific sequence. As a member of the peptide compound category, it embodies unique structural and stereochemical features that render it valuable for a variety of biochemical investigations. The incorporation of the D-enantiomer of leucine imparts resistance to proteolytic degradation, distinguishing this tripeptide from its all-L counterparts and enhancing its stability in diverse experimental contexts. Its defined sequence and chiral configuration make it particularly relevant for research focused on peptide transport, enzymatic specificity, and structure-activity relationships within peptide-based systems.
Peptide transport studies: D-Leucylglycylglycine is frequently employed as a model substrate in investigations of peptide transporter mechanisms, particularly those involving the oligopeptide transporter families such as PEPT1 and PEPT2. Its defined tripeptide structure and inclusion of a D-amino acid residue enable researchers to probe the substrate specificity and stereoselectivity of these transporters in cellular and membrane systems. Utilizing this compound facilitates the elucidation of transport kinetics, competitive inhibition, and the role of peptide structure in modulating uptake efficiency, thereby advancing understanding of nutrient absorption and drug delivery pathways.
Enzyme substrate specificity assays: The tripeptide serves as a valuable tool for characterizing the activity and selectivity of peptidases, including aminopeptidases, carboxypeptidases, and dipeptidyl peptidases. The presence of a D-leucine residue at the N-terminus challenges the substrate recognition capabilities of these enzymes, allowing researchers to assess their tolerance for non-canonical amino acid configurations. Such studies are instrumental in mapping active site preferences, delineating mechanisms of enzymatic discrimination, and guiding the design of protease-resistant peptide analogs for further research applications.
Peptide stability and degradation research: Due to its resistance to standard proteolytic cleavage, D-Leucylglycylglycine is often utilized in experiments designed to investigate peptide stability under physiological and experimental conditions. By comparing its degradation profile with those of all-L tripeptides, researchers can quantify the impact of D-amino acid incorporation on peptide half-life, susceptibility to enzymatic hydrolysis, and overall metabolic fate. These insights are critical for the rational design of stable peptide-based probes, biochemical reagents, and delivery vectors in research settings.
Analytical method development: The compound is also applied as a reference standard or calibration substrate in chromatographic and mass spectrometric analyses of peptide mixtures. Its defined sequence and unique stereochemical properties make it an ideal candidate for validating separation protocols, optimizing detection parameters, and assessing instrument sensitivity in peptide quantification workflows. The use of such synthetic tripeptides supports the development of robust analytical methodologies for peptide identification, purity assessment, and quality control in research laboratories.
Peptide structure-activity relationship (SAR) studies: D-Leucylglycylglycine provides a versatile scaffold for probing the relationship between peptide sequence, stereochemistry, and biological activity. By systematically varying the configuration or sequence of constituent amino acids, researchers can investigate how structural modifications influence binding affinity, receptor activation, or functional efficacy in biochemical assays. These SAR studies underpin the development of novel peptide-based probes, molecular tools, and research reagents tailored to specific experimental objectives.
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