N-Acetyl Lysyltyrosylcysteine Amide presents a tripeptide bearing nucleophilic, aromatic, and thiol functionalities under an N-acetyl cap. Lysine provides positive charge, tyrosine contributes π-systems and redox-active hydroxyl, while cysteine enables disulfide bonding and metal coordination. Researchers probe its reactivity in redox and conjugation reactions. Applications include antioxidant-motif studies, bioorganic chemistry, and peptide-thiol bioconjugation.
CAT No: R2543
CAS No:1287585-40-3
Synonyms/Alias:N-acetyl lysyltyrosylcysteine amide;1287585-40-3;SCHEMBL15862922;EX-A8001K;AKOS040756208;PD167056;TS-08889;HY-125039;CS-0088748;(2S)-2-acetamido-6-amino-N-[(2S)-1-[[(2R)-1-amino-1-oxo-3-sulfanylpropan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]hexanamide;
N-acetyl lysyltyrosylcysteine amide is a synthetic tripeptide composed of N-acetylated lysine, tyrosine, and cysteine residues, terminated with an amide group. This compound is structurally engineered to combine the functional side chains of basic, aromatic, and thiol-containing amino acids, providing a versatile molecular scaffold for biochemical research. Its unique sequence and post-synthetic modifications confer specific physicochemical properties, making it a valuable tool for probing peptide structure-activity relationships, redox biology, and peptide-based functional studies. As a custom-designed peptide, it is of significant interest in studies involving peptide stability, reactivity, and bioanalytical assay development.
Peptide structure-activity relationship studies: The tripeptide's defined sequence, featuring both N-terminal acetylation and C-terminal amidation, makes it highly relevant for investigating how chemical modifications influence peptide conformation and biological function. Researchers utilize this molecule to systematically assess the impact of terminal modifications on peptide folding, receptor interactions, and resistance to enzymatic degradation. Such studies are crucial for optimizing peptide-based ligands, biosensors, and molecular probes in basic and applied research settings.
Redox biochemistry research: The presence of a cysteine residue within the peptide's sequence introduces a reactive thiol group, which serves as a model for studying thiol-disulfide chemistry and redox mechanisms in peptides. Investigators leverage this property to explore oxidative folding, disulfide bond formation, and the role of cysteine-containing peptides in cellular redox regulation. By providing a controlled system for monitoring thiol reactivity, the compound supports the development of redox-sensitive assays and contributes to understanding redox signaling pathways.
Peptide modification and conjugation studies: The functional side chains of lysine, tyrosine, and cysteine enable selective chemical labeling, crosslinking, or conjugation with various reporter groups. Scientists employ this tripeptide as a substrate in method development for site-specific modification, including biotinylation, fluorescent tagging, or attachment to solid supports. Such applications are instrumental in the design of peptide-based affinity reagents, surface immobilization strategies, and bioanalytical platforms.
Enzyme substrate and inhibitor screening: The sequence of lysine, tyrosine, and cysteine residues provides recognition sites for multiple classes of proteolytic enzymes and post-translational modification enzymes such as kinases or acetyltransferases. The tripeptide can be used as a model substrate in enzyme assays to evaluate substrate specificity, catalytic efficiency, or inhibitor potency. These studies inform enzyme mechanism research and support the identification of novel modulators for biochemical pathways.
Analytical method development: The well-defined structure and functional diversity of N-acetyl lysyltyrosylcysteine amide make it a valuable reference standard or calibration compound in peptide quantification and detection techniques. Analytical chemists utilize it to optimize protocols for high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis. Its use in method validation ensures accuracy and reproducibility in peptide analytics, facilitating robust data generation for both research and quality control environments.
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