Me-Tyr-D-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Orn-Val-Leu-Abu-Gln-Leu-Ser-Ala-Arg-Orn-Leu-Leu-Gln-Asp-Ile-Nle-Asp-Arg-NHMe forms a long peptide chain featuring methylated residues, D-amino acids, and noncanonical components. Complex side-chain diversity shapes folding, charge distribution, and backbone rigidity. The sequence serves as a model for multivalent binding and extended conformational landscapes. Applications include structural biology, peptide engineering, and motif-function investigation.
CAT No: R2435
CAS No:1445155-39-4
Synonyms/Alias:Me-Tyr-D-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Orn-Val-Leu-Abu-Gln-Leu-Ser-Ala-Arg-Orn-Leu-Leu-Gln-Asp-Ile-Nle-Asp-Arg-NHMe;1445155-39-4;MR 409;
Me-Tyr-D-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Orn-Val-Leu-Abu-Gln-Leu-Ser-Ala-Arg-Orn-Leu-Leu-Gln-Asp-Ile-Nle-Asp-Arg-NHMe is a synthetic peptide characterized by a unique sequence featuring both natural and non-natural amino acids, including N-methylated and D-amino acid residues. This structural complexity imparts enhanced enzymatic stability and potential for diverse bioactivity, making it a valuable tool for scientific research. The presence of unusual residues such as Abu (2-aminobutyric acid), Orn (ornithine), Nle (norleucine), and N-methyl modifications further expands its utility in exploring structure-activity relationships and protein interactions. Researchers are drawn to this peptide due to its resistance to proteolytic degradation and its capacity to mimic or disrupt native biological processes, supporting advanced investigations in molecular biology, biochemistry, and peptide engineering.
Peptide-protein interaction studies: Me-Tyr-D-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Orn-Val-Leu-Abu-Gln-Leu-Ser-Ala-Arg-Orn-Leu-Leu-Gln-Asp-Ile-Nle-Asp-Arg-NHMe serves as a powerful probe in elucidating the binding dynamics between peptides and target proteins. Its sequence diversity, including D-amino acid and N-methyl modifications, enables researchers to assess how structural alterations influence affinity, specificity, and binding kinetics. By employing this peptide in pull-down assays, surface plasmon resonance, or isothermal titration calorimetry, scientists can gain insights into the molecular mechanisms of protein recognition and interaction, which is fundamental for understanding cellular signaling pathways and the development of novel modulators.
Enzyme substrate and inhibitor research: The synthetic peptide's modified residues confer resistance to common proteases, making it an excellent substrate or competitive inhibitor in enzymatic assays. Researchers can use it to evaluate the specificity and catalytic efficiency of various proteolytic enzymes, or to screen for novel inhibitors that target protease active sites. Its stability allows for prolonged assay times and reliable measurement of enzymatic activity, facilitating the identification of key determinants in enzyme-substrate recognition and the development of enzyme-targeted research tools.
Peptide structure-function analysis: Me-Tyr-D-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Orn-Val-Leu-Abu-Gln-Leu-Ser-Ala-Arg-Orn-Leu-Leu-Gln-Asp-Ile-Nle-Asp-Arg-NHMe is frequently utilized in structure-activity relationship (SAR) studies, where systematic modifications to the peptide backbone provide insights into the relationship between sequence, conformation, and biological function. The inclusion of non-standard amino acids such as Abu, Orn, and Nle permits the exploration of side-chain contributions to peptide folding, stability, and target interaction. Advanced techniques like NMR spectroscopy, circular dichroism, and molecular modeling can be applied to this peptide to characterize its secondary structure and dynamic behavior in solution.
Cell signaling pathway investigation: The robust stability and tailored sequence of this peptide make it suitable for probing cellular signaling pathways in vitro. Researchers can introduce the peptide into cultured cells to evaluate its impact on downstream effectors, receptor activation, or intracellular signaling cascades. Its resistance to degradation ensures that observed biological effects are attributable to the intact molecule, thereby providing reliable data for dissecting complex regulatory networks and identifying novel signaling modulators.
Biomaterial and drug delivery research: The unique physicochemical properties of Me-Tyr-D-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Orn-Val-Leu-Abu-Gln-Leu-Ser-Ala-Arg-Orn-Leu-Leu-Gln-Asp-Ile-Nle-Asp-Arg-NHMe, including its stability and sequence versatility, make it an attractive candidate for biomaterial engineering and drug delivery system development. Scientists can integrate it into hydrogels, nanoparticles, or other delivery platforms to investigate its role in modulating material properties or facilitating targeted delivery. Its functional groups offer multiple sites for conjugation or modification, enabling tailored interactions with biological environments and supporting innovative approaches in material science and therapeutic research.
2. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
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5. Immune-awakening Saccharomyces-inspired nanocarrier for oral target delivery to lymph and tumors
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