c(Bua-Cpa-Thi-Val-Asn-Cys)-Pro-d-Arg-NEt2 is a potent, selective and short-acting peptidic V2 receptor (V2R) agonist with EC50s of 0.07 and 0.02 nM for hV2R and rV2R, respectively.
c(Bua-Cpa-Thi-Val-Asn-Cys)-Pro-d-Arg-NEt2 is a synthetic cyclic peptide featuring a distinctive sequence and conformationally constrained backbone, designed to facilitate advanced research in peptide science and molecular biology. Its unique arrangement of non-standard and standard amino acid residues, alongside cyclization, imparts enhanced stability and distinct biochemical properties. As a research-grade peptide, it offers valuable opportunities for probing structure-activity relationships, molecular recognition events, and functional modulation in a range of biochemical contexts. The presence of both natural and modified residues, as well as a C-terminal diethylamide modification, broadens its utility in experimental design, making it a versatile tool for investigating peptide structure and function.
Peptide structure-activity relationship studies: The cyclic nature and tailored sequence of this peptide make it highly suitable for elucidating the relationship between peptide conformation and biological activity. Researchers can employ it as a model system to investigate how backbone cyclization and side-chain modifications influence receptor binding, enzymatic stability, or target selectivity. By systematically comparing analogues or introducing site-specific modifications, the compound serves as a reference point for understanding the critical determinants of peptide-mediated interactions.
Molecular recognition and binding assays: Owing to its defined three-dimensional structure and the presence of both hydrophobic and polar residues, this cyclic peptide is an effective probe for studying molecular recognition mechanisms. It can be utilized in binding assays to characterize interactions with protein targets, nucleic acids, or other biomolecules. Such studies are pivotal for mapping binding epitopes, quantifying affinity constants, and dissecting the influence of conformational rigidity on molecular recognition events.
Protease resistance and metabolic stability evaluation: The cyclized backbone and incorporation of non-canonical residues confer increased resistance to proteolytic degradation, making the peptide an excellent candidate for experiments focused on metabolic stability. By subjecting it to various protease-rich environments or cellular extracts, researchers can assess degradation kinetics and compare stability profiles against linear or unmodified sequences. These insights are crucial for the rational design of peptides with enhanced in vitro or ex vivo persistence.
Peptide-protein interaction mapping: The sequence diversity and conformational constraints of this compound render it valuable for mapping interaction surfaces between peptides and protein partners. It can be deployed in pull-down assays, surface plasmon resonance, or other biophysical techniques to delineate binding regions, identify interacting residues, and quantify binding dynamics. Such applications are instrumental in advancing the understanding of protein-peptide interfaces and guiding the development of novel modulators or inhibitors.
Peptide synthesis and analytical validation: The complexity and modifications present in this cyclic peptide also make it a useful standard for evaluating peptide synthesis methodologies and analytical techniques. It can serve as a challenging substrate for testing cyclization strategies, side-chain protection schemes, and purification protocols. Additionally, its defined structure and mass are advantageous for validating analytical platforms such as HPLC, mass spectrometry, or NMR, supporting quality control and method development in peptide chemistry laboratories.
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