H-Gly-Leu-Met-NH2·HCl is a tripeptide amide featuring a hydrophobic-sulfur-containing residue arrangement. Methionine offers redox-sensitive functionality, while the amide terminus stabilizes charge. Researchers use it to explore folding dynamics and redox-driven conformational changes. Applications include peptide-stability studies, model-substrate research, and structural profiling.
CAT No: R2401
CAS No:40297-96-9
Synonyms/Alias:H-Gly-Leu-Met-Nh2 HCl;40297-96-9;H-Gly-Leu-Met-NH2.HCl;(2S)-2-[(2-aminoacetyl)amino]-N-[(2S)-1-amino-4-methylsulfanyl-1-oxobutan-2-yl]-4-methylpentanamide;hydrochloride;(S)-N-((S)-1-Amino-4-(methylthio)-1-oxobutan-2-yl)-2-(2-aminoacetamido)-4-methylpentanamide hydrochloride;H-Gly-Leu-Met-NH2-HCl;HGly-Leu-MetNH2 hydrochloride;H-Gly-leu-met-nh2 hydrochloride;MBMAGTQNPFSIDF-IYPAPVHQSA-N;glycyl-leucyl-methioninamide hydrochloride;AS-87035;G85273;
H-Gly-Leu-Met-Nh2 HCl is a synthetic peptide composed of glycine, leucine, and methionine in a specific sequence, terminated with an amide group and supplied as its hydrochloride salt. As a tripeptide, it represents a valuable tool in peptide biochemistry, offering a defined structure suitable for mechanistic studies and functional analyses. Its sequence and chemical modifications render it particularly relevant for investigations into peptide bond formation, stability, and biological mimicry, making it a versatile component in research focused on peptide-protein interactions, enzymatic processing, and structure-activity relationships.
Peptide synthesis validation: In the context of solid-phase peptide synthesis (SPPS) and solution-phase peptide assembly, H-Gly-Leu-Met-Nh2 HCl serves as a reference standard for evaluating synthetic methodologies and optimizing coupling efficiencies. Its defined sequence and terminal modifications enable researchers to assess the fidelity of peptide chain elongation, monitor side reactions, and validate deprotection strategies. The tripeptide is frequently employed as a model substrate for benchmarking resin performance or testing new coupling reagents, thereby supporting the advancement of peptide chemistry techniques.
Enzymatic substrate studies: Owing to its compact size and specific amino acid sequence, this tripeptide is an ideal substrate for characterizing the activity and specificity of various proteolytic enzymes, such as exopeptidases and endopeptidases. Researchers utilize it to dissect cleavage preferences, kinetic parameters, and substrate-enzyme interactions under controlled conditions. Such studies are crucial for elucidating the mechanistic basis of peptide hydrolysis and for developing selective inhibitors or modulators of protease function.
Peptide-protein interaction analysis: The defined structure of Gly-Leu-Met-NH2 facilitates its use in probing non-covalent interactions with target proteins, including binding assays and affinity measurements. By incorporating the tripeptide into binding studies, scientists can investigate recognition motifs, map interaction surfaces, and quantify binding affinities relevant to both fundamental research and the design of peptide-based probes. These analyses contribute to a deeper understanding of molecular recognition processes in biological systems.
Structural and conformational research: Due to its short length and terminal modifications, the tripeptide is well-suited for spectroscopic and crystallographic studies aimed at elucidating peptide backbone conformations and side chain orientations. Researchers employ it in nuclear magnetic resonance (NMR), circular dichroism (CD), and X-ray crystallography experiments to model peptide folding, hydrogen bonding patterns, and the impact of specific residues on overall structure. Insights gained from these studies inform the design of more complex peptide analogs with tailored properties.
Analytical method development: H-Gly-Leu-Met-Nh2 HCl is also frequently utilized as a calibration standard or test analyte in the development and validation of analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry (MS). Its well-characterized physicochemical properties make it suitable for optimizing detection parameters, assessing chromatographic separation efficiency, and calibrating quantitative assays. The use of such model peptides enhances the reliability and reproducibility of analytical workflows in peptide research and quality control environments.
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