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 comprised of a defined sequence of amino acids, including both natural and non-natural residues. Distinguished by the presence of Mpa (3-mercaptopropionic acid) at the N-terminus and a C-terminal amidation, this peptide exhibits unique structural features that influence its biochemical properties and potential functionality. The inclusion of D-arginine, alongside a strategically positioned cysteine, further enhances its conformational stability and resistance to proteolytic degradation, making it a versatile tool for advanced peptide research. Its sequence design allows for exploration of structure-activity relationships, receptor interactions, and molecular recognition phenomena relevant to peptide science and molecular biology.
Peptide structure-activity relationship studies: Researchers frequently employ this peptide in investigations aimed at elucidating the relationship between primary amino acid sequence and biological activity. The incorporation of both D-amino acids and non-standard modifications enables systematic evaluation of how these alterations affect receptor binding, conformational dynamics, and bioactivity profiles. Such studies are critical for the rational design of peptide-based probes, ligands, or inhibitors, and for advancing the understanding of molecular determinants governing peptide function.
Receptor binding assays: The defined sequence and chemical modifications of this peptide make it suitable for use in receptor binding studies, particularly when probing the specificity and affinity of peptide-protein interactions. Its stability and tailored side-chain functionalities facilitate the mapping of binding epitopes on target receptors, offering valuable insights into ligand recognition, signal transduction mechanisms, and the development of selective modulators for research applications.
Peptide synthesis and method validation: As a synthetic standard, this peptide serves as a useful reference for validating solid-phase peptide synthesis protocols and analytical techniques such as HPLC and mass spectrometry. Its sequence complexity, including the presence of a terminal amide and non-canonical residues, challenges synthetic workflows and analytical detection methods, providing a robust benchmark for quality control and method optimization in peptide chemistry laboratories.
Biochemical probe development: The unique physicochemical properties of this peptide, conferred by its sequence and modifications, make it an attractive candidate for the development of specialized biochemical probes. By incorporating functional groups amenable to conjugation or labeling, it can be adapted for applications such as fluorescence-based detection, affinity purification, or immobilization on biosensor platforms, thereby expanding the toolkit available for studying protein-peptide interactions and cellular signaling pathways.
Enzyme substrate studies: Due to the presence of specific amino acid motifs and modifications, this peptide can be utilized as a substrate in enzymatic assays designed to investigate protease specificity, cleavage efficiency, or post-translational modification processes. Its resistance to nonspecific degradation and defined sequence allow for precise monitoring of enzyme activity, supporting the development of new assay formats and the characterization of proteolytic mechanisms within complex biological systems.
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