N-[(6S)-6-Carboxy-6-(glycylamino)hexanoyl]-D-alanyl-D-alanine

N-[(6S)-6-Carboxy-6-(glycylamino)hexanoyl]-D-alanyl-D-alanine, a paramount peptide derivative characterized by its intricate composition, finds indispensable utility within the biomedical arena as a potent remedy against bacterial infections. Through its targeted mechanism of action in impeding the synthesis of bacterial cell walls, this exceptional compound exerts its efficacious influence upon an array of drug-resistant strains. Consequently, it emerges as a promising therapeutic paradigm for the combat against the pernicious onslaught of drug-resistant bacterial diseases.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: R2036

CAS No:306748-45-8

Chemical Name:(2S)-2-amino-7-[(2-aminoacetyl)-[(2R)-1-[[(1R)-1-carboxyethyl]amino]-1-oxopropan-2-yl]amino]-7-oxoheptanoic acid

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cGMP Peptide
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M.F/Formula
C15H26N4O7
M.W/Mr.
374.39

N-[(6S)-6-Carboxy-6-(glycylamino)hexanoyl]-D-alanyl-D-alanine is a synthetic peptide derivative characterized by a specific sequence and stereochemistry, making it a valuable tool for advanced biochemical research. As a structurally defined tripeptide containing both D-alanine residues and a modified hexanoyl moiety, it serves as a model compound for investigations into peptide structure-activity relationships, enzymatic recognition, and metabolic processing. Its unique configuration, including the presence of both carboxylic and amino functional groups, enables exploration of peptide interactions and stability under various experimental conditions. Researchers utilize this compound to probe fundamental questions in peptide chemistry and to support the development of new methodologies in peptide synthesis and analysis.

Peptide substrate studies: Due to its defined sequence and stereochemistry, this compound is frequently employed as a substrate in enzymatic assays, particularly those targeting peptidases and proteases with specificity for D-alanyl residues or modified peptide termini. Its structure allows researchers to monitor enzyme-substrate interactions, assess catalytic efficiency, and elucidate mechanisms of peptide bond hydrolysis. Such studies are essential for characterizing enzyme specificity, mapping active sites, and developing novel inhibitors or probes for biochemical pathways involving D-amino acid-containing peptides.

Peptide transport and uptake research: The presence of D-alanyl-D-alanine motifs makes this tripeptide an ideal probe for investigating the mechanisms of peptide transport across biological membranes. It is commonly used in studies of bacterial and eukaryotic peptide transporters, enabling the evaluation of substrate recognition, uptake kinetics, and competitive inhibition profiles. By tracing the movement and cellular handling of this compound, scientists gain insights into the selectivity and regulatory features of peptide transport systems, which are critical for understanding nutrient acquisition, signaling, and resistance mechanisms in microbial physiology.

Peptidomimetic design and structure-activity relationship analysis: The modified hexanoyl group and the incorporation of D-amino acids render this molecule a valuable scaffold in the design and evaluation of peptidomimetics. Researchers utilize it to systematically vary side chains and backbone configurations, allowing for the assessment of how structural modifications influence biological activity, stability, and receptor binding. Studies leveraging this compound contribute to the rational development of peptide-based tools and potential modulators for biochemical applications, including enzyme inhibition and receptor targeting.

Analytical method development: The unique chemical properties and defined sequence of this tripeptide make it a useful standard or reference compound in the development and validation of analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis. Its stability and detectability facilitate calibration, method optimization, and the assessment of assay sensitivity and specificity when quantifying peptides or monitoring peptide modifications in complex biological samples.

Peptide synthesis optimization: As a structurally complex peptide incorporating both D- and L-amino acids, this compound serves as a benchmark for evaluating synthetic methodologies in solid-phase peptide synthesis (SPPS) and solution-phase approaches. Researchers use it to test coupling efficiency, stereochemical fidelity, and purification strategies, providing critical feedback for improving synthesis protocols. Its successful assembly and characterization help optimize conditions for producing challenging peptide sequences, ultimately supporting the advancement of peptide chemistry and the reliable production of research-grade peptides.

InChI
InChI=1S/C15H26N4O7/c1-8(14(23)24)18-13(22)9(2)19(12(21)7-16)11(20)6-4-3-5-10(17)15(25)26/h8-10H,3-7,16-17H2,1-2H3,(H,18,22)(H,23,24)(H,25,26)/t8-,9-,10+/m1/s1
InChI Key
OMRBEOKVIPPVRT-BBBLOLIVSA-N
Canonical SMILES
CC(C(=O)O)NC(=O)C(C)N(C(=O)CCCCC(C(=O)O)N)C(=O)CN
Isomeric SMILES
C[C@H](C(=O)O)NC(=O)[C@@H](C)N(C(=O)CCCC[C@@H](C(=O)O)N)C(=O)CN

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