Mpa-Tyr-Phe-Gln-Asn-Cys-Pro-D-Arg-Gly-NH2 features a sequence enriched with aromatic, polar, and basic residues, contributing to diverse interaction modes. The presence of cysteine introduces opportunities for disulfide-mediated stability. Researchers examine its folding and solvent-dependent conformations. Applications include peptide engineering, structural analysis, and motif-function mapping.
CAT No: R2684
CAS No:119364-41-9
Synonyms/Alias:CHEMBL265919;SCHEMBL8193601;EX-A9231;Mpa-Tyr-Phe-Gln-Asn-Cys-Pro-D-Arg-Gly-NH2;119364-41-9;
Mpa-Tyr-Phe-Gln-Asn-Cys-Pro-D-Arg-Gly-NH2 is a synthetic peptide featuring a unique sequence that combines both natural and non-natural amino acids, including a D-arginine residue and an amidated C-terminus. The presence of the Mpa (mercaptopropionyl) group at the N-terminus, along with the specific arrangement of amino acids, imparts distinctive physicochemical and biological properties to the molecule. This peptide is valued in research for its stability, resistance to enzymatic degradation, and potential for diverse functionalization, making it a versatile tool in scientific investigations. Its structural features enable researchers to explore molecular interactions, signaling pathways, and receptor binding with enhanced specificity and control, supporting a wide range of innovative applications across the biochemical and life sciences fields.
Peptide-receptor interaction studies: Mpa-Tyr-Phe-Gln-Asn-Cys-Pro-D-Arg-Gly-NH2 is frequently employed in receptor binding assays to elucidate the molecular mechanisms underlying peptide recognition and signal transduction. The inclusion of D-arginine and the C-terminal amidation increase its resistance to proteolytic enzymes, allowing for more accurate measurement of binding kinetics and affinity in both in vitro and in vivo systems. By serving as a model ligand, this peptide facilitates the identification of key amino acid residues involved in receptor activation or inhibition, providing valuable insights into the structural requirements for selective receptor modulation.
Enzyme substrate profiling: In enzymology research, the peptide serves as a well-defined substrate for characterizing the specificity and catalytic activity of various proteases and peptidases. Its unique sequence, particularly the presence of a disulfide-capable cysteine and the non-standard D-arginine, enables researchers to assess enzyme-substrate interactions under different conditions. By monitoring the cleavage patterns and rates, scientists can better understand enzyme selectivity, substrate preferences, and potential regulatory mechanisms, which are critical for developing enzyme inhibitors or activators for research and therapeutic exploration.
Structure-activity relationship (SAR) analysis: Mpa-Tyr-Phe-Gln-Asn-Cys-Pro-D-Arg-Gly-NH2 is instrumental in SAR studies aimed at dissecting the functional contributions of individual amino acid residues and modifications. Researchers can introduce targeted substitutions or chemical modifications at specific positions within the peptide to evaluate changes in biological activity, stability, or receptor affinity. These systematic investigations contribute to the rational design of novel peptides with optimized properties for use as research probes, molecular tools, or potential therapeutic leads.
Peptide conjugate development: The presence of functional groups such as the N-terminal Mpa and the cysteine residue allows for site-specific conjugation of the peptide to various molecular entities, including fluorescent dyes, biotin, or nanoparticles. Such conjugates are widely used in imaging, affinity purification, or targeted delivery studies. By leveraging the modular nature of the peptide, scientists can create multifunctional constructs that enable precise tracking, detection, or manipulation of biological targets in complex systems.
Cell signaling pathway exploration: The sequence of Mpa-Tyr-Phe-Gln-Asn-Cys-Pro-D-Arg-Gly-NH2 is particularly useful in dissecting signal transduction mechanisms mediated by peptide ligands. When introduced into cellular models, it can activate or inhibit specific pathways, allowing researchers to map downstream signaling events and identify key regulatory nodes. The peptide's stability and resistance to degradation ensure sustained activity, supporting detailed time-course analyses and mechanistic studies in diverse biological contexts.
Biomolecular interaction mapping: Researchers utilize this synthetic peptide as a probe for mapping interactions with proteins, nucleic acids, or other biomolecules in vitro. Its defined structure and modifiable groups facilitate the development of cross-linking or pull-down assays, which are essential for identifying binding partners and elucidating complex formation in cellular extracts or purified systems. Through such applications, Mpa-Tyr-Phe-Gln-Asn-Cys-Pro-D-Arg-Gly-NH2 advances the understanding of molecular networks and interaction dynamics, supporting the discovery of novel regulatory mechanisms and potential intervention points in biological pathways.
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