Leu-Trp-OMe HCl joins hydrophobic leucine with aromatic tryptophan in a methyl ester format that aids hydrolysis studies. The indole ring provides a spectroscopic handle for interaction analysis. Protonation in the hydrochloride form enhances solubility. Research uses include peptide coupling optimization, binding studies, and conformational modeling.
CAT No: R2455
CAS No:143413-36-9
Synonyms/Alias:LEU-TRP-OME HCL;143413-36-9;H-Leu-Trp-OMe.HCl;MFCD00155480;L-Tryptophan, N-L-leucyl-, methyl ester, monohydrochloride;Leu-trp-ome hydrochloride;(L)-Leu-(L)-TrpOMe.HCl;UWXXREJDKHROOB-DMLYUBSXSA-N;AT16952;L-Tryptophan, L-leucyl-, methyl ester, hydrochloride (1:1);methyl (2S)-2-[[(2S)-2-amino-4-methylpentanoyl]amino]-3-(1H-indol-3-yl)propanoate;hydrochloride;
Leu-trp-ome HCl, also known as Leucyltryptophylornithine hydrochloride, is a synthetic tripeptide derivative that has garnered interest in the fields of biochemical research and peptide science. Characterized by its unique sequence of leucine, tryptophan, and ornithine, this compound is typically supplied as a hydrochloride salt to enhance its solubility and stability in aqueous environments. Its structural configuration offers a balance between hydrophobic and basic amino acid residues, making it a versatile tool for probing peptide interactions, enzymatic processing, and receptor binding studies. Due to its defined molecular architecture, Leu-trp-ome HCl serves as a valuable model compound for exploring peptide behavior, conformational dynamics, and structure-activity relationships in various biochemical contexts.
Peptide-Protein Interaction Studies: Leu-trp-ome HCl is frequently utilized in research focused on elucidating the mechanisms of peptide-protein interactions. Its specific amino acid sequence allows scientists to investigate binding affinities, recognition motifs, and the influence of side-chain chemistry on protein docking. By incorporating this tripeptide into binding assays or using it as a competitive inhibitor in affinity studies, researchers can gain insights into the molecular determinants governing selective recognition between peptides and target proteins. Such studies contribute to the rational design of peptide-based ligands and the understanding of protein function at a molecular level.
Enzymatic Substrate Characterization: In enzymology, Leucyltryptophylornithine hydrochloride serves as a substrate for analyzing the specificity and catalytic efficiency of various peptidases and proteases. Its sequence, featuring both hydrophobic and basic residues, provides a relevant model for assessing how enzymes recognize and cleave peptide bonds. Researchers employ this compound to determine kinetic parameters, map active sites, and elucidate substrate preferences, thereby advancing the knowledge of enzyme mechanisms and supporting the development of selective enzyme inhibitors for research applications.
Peptide Transport and Uptake Studies: The unique properties of Leu-trp-ome HCl make it suitable for investigating peptide transport mechanisms across biological membranes. By labeling or modifying this tripeptide, scientists can track its uptake and distribution in cellular or tissue models, shedding light on the function of peptide transporters and the factors that modulate their activity. These studies are essential for understanding nutrient absorption, peptide-based drug delivery, and the physiological roles of oligopeptide transport systems.
Structure-Activity Relationship (SAR) Analysis: Leu-trp-ome HCl is an effective tool in SAR studies aimed at deciphering how modifications to peptide sequence impact biological activity. Researchers synthesize analogs or derivatives of this tripeptide to systematically alter side-chain properties, backbone conformation, or terminal groups. By comparing the activity profiles of different variants, scientists can identify key structural features responsible for target engagement, stability, or bioavailability, facilitating the optimization of peptide-based research probes and molecular scaffolds.
Analytical Method Development: The defined composition and physicochemical characteristics of Leu-trp-ome HCl make it an ideal standard or reference compound in the development and calibration of analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry (MS). Its use enables accurate quantification, method validation, and troubleshooting in peptide analysis workflows, ensuring reliability and reproducibility in research settings. Through these diverse applications, Leu-trp-ome HCl continues to play a pivotal role in advancing peptide science and supporting innovation across multiple domains of biochemical research.
4. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
5. Peptides as Active Ingredients: A Challenge for Cosmeceutical Industry
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