Z-Gly-Gly-Phe-OH is a protected tripeptide featuring a benzyloxycarbonyl cap that regulates N-terminal reactivity. Glycine enhances flexibility while phenylalanine provides aromatic stabilization. Researchers employ it in fragment-coupling studies and synthetic intermediate development. Applications include SPPS planning, building-block libraries, and peptidomimetic design.
CAT No: R2373
CAS No:13171-93-2
Synonyms/Alias:Z-Gly-Gly-Phe-OH;13171-93-2;(S)-11-Benzyl-3,6,9-trioxo-1-phenyl-2-oxa-4,7,10-triazadodecan-12-oic acid;(2S)-2-[2-(2-{[(BENZYLOXY)CARBONYL]AMINO}ACETAMIDO)ACETAMIDO]-3-PHENYLPROPANOIC ACID;((Benzyloxy)carbonyl)glycylglycyl-L-phenylalanine;MFCD00055796;Z-Gly-Gly-Phe;Cbz-Gly-Gly-L-Phe;SCHEMBL11239042;BDBM36228;PARPWSYTROKYNG-KRWDZBQOSA-N;AKOS022180797;carbobenzoxyglycylglycyl-l-phenylalanine;HY-W090942;AS-56825;FG111472;CS-0134047;E86793;L-Phenylalanine,N-[(phenylmethoxy)carbonyl]glycylglycyl-(9ci);(S)-11-Benzyl-3,6,9-trioxo-1-phenyl-2-oxa-4,7,10-triazadodecan-12-oicacid;
Z-Gly-Gly-Phe-OH, also known as N-carbobenzoxy-glycyl-glycyl-phenylalanine, is a synthetic peptide featuring a protected N-terminus and a free carboxylic acid group at the C-terminus. This tripeptide derivative is frequently utilized in biochemical research due to its well-defined structure and versatility in peptide synthesis. Its carbobenzoxy (Z) group serves as a protective moiety, safeguarding the amino group from undesired reactions during sequential peptide elongation. The combination of glycine and phenylalanine residues within its sequence provides both flexibility and hydrophobic interaction potential, making it an attractive model for investigating peptide behavior, enzyme specificity, and structure-activity relationships in various experimental settings.
Peptide Synthesis Research: Z-Gly-Gly-Phe-OH is widely employed as a building block or intermediate in the solid-phase and solution-phase synthesis of longer peptides. Its protected amino terminus allows for selective deprotection and coupling steps, facilitating the assembly of complex peptide chains with high yield and fidelity. Researchers often use it to study the efficiency of different coupling reagents, optimize synthetic protocols, and develop novel methodologies for peptide bond formation. By incorporating this tripeptide into larger sequences, scientists can assess the impact of glycine and phenylalanine residues on the overall conformation and reactivity of synthetic peptides, contributing valuable insights to the field of peptide chemistry.
Enzyme Substrate Studies: As a model substrate, N-carbobenzoxy-glycyl-glycyl-phenylalanine is instrumental in evaluating the specificity and kinetics of proteolytic enzymes, particularly those that recognize aromatic or small neutral residues. By monitoring the enzymatic hydrolysis of this peptide, researchers can determine the substrate preferences of various proteases, such as chymotrypsin or trypsin, and elucidate mechanisms of peptide bond cleavage. These studies are essential for understanding enzyme-substrate interactions, designing selective inhibitors, and characterizing novel proteolytic activities in biological samples.
Structure-Activity Relationship Analysis: The defined sequence and protective group of Z-Gly-Gly-Phe-OH make it an ideal candidate for investigating how structural modifications influence biological activity. Scientists can systematically alter the peptide's sequence or protective groups and assess the resulting changes in function, stability, or interaction with other biomolecules. This approach provides a foundation for rational drug design, the development of peptidomimetics, and the engineering of peptides with tailored properties for research or industrial applications.
Analytical Method Development: Glycyl-glycyl-phenylalanine derivatives are frequently used as standards or calibration materials in chromatographic and spectrometric techniques. Their predictable behavior during high-performance liquid chromatography (HPLC) or mass spectrometry enables accurate method validation, instrument calibration, and quantification of peptide samples. By incorporating Z-Gly-Gly-Phe-OH into analytical workflows, laboratories can ensure the reliability and reproducibility of peptide detection, separation, and characterization processes.
Biophysical and Conformational Studies: The unique combination of glycine's flexibility and phenylalanine's aromaticity in this tripeptide provides a valuable model for probing peptide folding, aggregation, and interaction with membranes or other macromolecules. Researchers utilize it to investigate the influence of sequence motifs on secondary structure formation, hydrophobic interactions, and peptide self-assembly. Such studies enhance our understanding of fundamental biophysical principles governing peptide behavior and inform the rational design of novel biomaterials and functional peptides for diverse scientific applications.
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