The eicosapeptide DSAPNPVLDIDGEKLRTGTN corresponds to the N-terminal sequence of the taste-modifying 191 amino acid-containing protein miraculin produced by the berries of Richadella dulcifica.
CAT No: R1924
CAS No:198694-37-0
Synonyms/Alias:198694-37-0;Miraculin (1-20);Miraculin (1-20) (H-Asp-Ser-Ala-Pro-Asn-Pro-Val-Leu-Asp-Ile-Asp-Gly-Glu-Lys-Leu-Arg-Thr-Gly-Thr-Asn-OH);MFCD00076869;DA-55498;
Chemical Name:(4S)-5-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-1-[[(2S,3R)-1-[[2-[[(2S,3R)-1-[[(1S)-3-amino-1-carboxy-3-oxopropyl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-2-oxoethyl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-4-[[2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-4-amino-2-[[(2S)-1-[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-carboxypropanoyl]amino]-3-hydroxypropanoyl]amino]propanoyl]pyrrolidine-2-carbonyl]amino]-4-oxobutanoyl]pyrrolidine-2-carbonyl]amino]-3-methylbutanoyl]amino]-4-methylpentanoyl]amino]-3-carboxypropanoyl]amino]-3-methylpentanoyl]amino]-3-carboxypropanoyl]amino]acetyl]amino]-5-oxopentanoic acid
Miraculin (1-20) is a synthetic peptide fragment derived from the N-terminal sequence of miraculin, a glycoprotein originally isolated from the fruit of Synsepalum dulcificum, commonly known as the miracle berry. As a peptide compound, Miraculin (1-20) comprises the first twenty amino acids of the native protein, enabling researchers to explore the structural and functional properties of this unique sequence. The peptide is of significant interest in biochemical and sensory research due to miraculin's well-documented ability to modulate taste perception, particularly its capacity to induce a sweet taste response in the presence of acidic conditions. By providing a defined segment of the full-length protein, Miraculin (1-20) offers a valuable tool for dissecting the molecular determinants underlying taste-modifying activity and for advancing peptide-based studies in sensory biology and protein engineering.
Peptide structure-function analysis: Miraculin (1-20) serves as a critical resource for investigating the relationship between primary sequence and bioactivity in taste-modifying proteins. Researchers utilize this peptide to identify which regions of miraculin are essential for its interaction with taste receptors, particularly the human sweet taste receptor complex. By systematically studying the N-terminal fragment, scientists can elucidate the minimal structural motifs required for receptor binding and activation, thereby advancing understanding of the molecular mechanisms that govern taste modulation.
Sensory biology research: The availability of Miraculin (1-20) enables targeted studies into the sensory transduction pathways involved in sweetness perception. By comparing the activity of this peptide fragment with longer or modified versions, investigators can map the regions of miraculin responsible for its pH-dependent sweet-inducing properties. Such comparative analyses contribute to a deeper comprehension of how specific peptide segments influence taste receptor signaling, facilitating the rational design of novel taste modulators or mimetics for research use.
Peptide synthesis and engineering: Miraculin (1-20) is frequently employed as a model substrate in peptide synthesis protocols, particularly for optimizing solid-phase peptide synthesis (SPPS) techniques. Its defined sequence provides a benchmark for evaluating coupling efficiency, protecting group strategies, and purification methodologies. Furthermore, the peptide's relevance to functional protein domains makes it a valuable template for engineering modified peptides with altered physicochemical properties or enhanced stability, supporting advances in peptide technology and synthetic biology.
Analytical method development: The defined structure of Miraculin (1-20) allows it to function as a reference standard in analytical chemistry applications such as high-performance liquid chromatography (HPLC) and mass spectrometry. Researchers utilize the peptide to calibrate instruments, validate separation protocols, and benchmark detection sensitivity for peptide-based analytes. Its use in these contexts supports rigorous method development and quality control in peptide research laboratories.
Biochemical interaction studies: The N-terminal fragment of miraculin is used to probe specific interactions with other biomolecules, including membrane proteins, receptors, and antibodies. By employing Miraculin (1-20) in binding assays or structural studies, researchers can characterize the specificity and affinity of peptide-protein interactions relevant to taste biology and protein recognition. These investigations provide foundational data for mapping epitope regions, understanding receptor-ligand dynamics, and informing the rational design of functional peptides for research applications.
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