cyclo[2Nal-Arg-D-Arg-Arg-D-Arg-Gln-D-Phe] forms a constrained cyclic peptide enriched with aromatic and basic residues. The mixed chirality enables exploration of stereochemical effects on ring topology. Researchers evaluate its binding behavior and conformational rigidity. Applications include receptor-binding studies, cyclic-peptide design, and structural motif research.
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CAT No: R2673
CAS No:1831064-63-1
Synonyms/Alias:CPP9;CHEMBL4754257;EX-A10042;HY-P10644;1831064-63-1;
Cyclo[2Nal-Arg-D-Arg-Arg-D-Arg-Gln-D-Phe] is a synthetic cyclic peptide featuring a unique sequence of alternating L- and D-amino acids, including the non-canonical 2-naphthylalanine (2Nal) residue. This structural configuration imparts the molecule with enhanced conformational rigidity and resistance to proteolytic degradation, making it a valuable tool in peptide research. Its design enables the exploration of structure-activity relationships, molecular recognition, and peptide-mimetic interactions, contributing to the broader understanding of peptide functionality in biochemical systems. The presence of both arginine and glutamine residues further supports its relevance in studies involving charge interactions and hydrogen bonding within peptide frameworks.
Peptide structure-activity relationship studies: The cyclic architecture and incorporation of both natural and non-natural amino acids in this peptide make it particularly well-suited for structure-activity relationship (SAR) investigations. Researchers leverage such molecules to systematically probe how sequence modifications, stereochemistry, and ring constraints influence biological activity, binding affinity, and molecular stability. The inclusion of D-amino acids, alongside the bulky 2Nal residue, provides a model system for dissecting the role of side-chain orientation and ring topology in modulating peptide interactions with target proteins or receptors.
Protease resistance evaluation: Cyclic peptides containing D-amino acids and non-standard residues are frequently employed as model substrates in proteolytic stability assays. By assessing the degradation profile of this compound in the presence of various proteases, scientists can gain insights into the mechanisms of enzymatic recognition and cleavage resistance. Such studies are instrumental in the rational design of peptide-based probes, diagnostics, and research tools that require extended biological half-life or enhanced resilience in complex biological environments.
Molecular recognition and binding studies: The amphipathic nature and charge distribution of this cyclic peptide, driven by multiple arginine residues and the hydrophobic 2Nal side chain, make it a compelling candidate for investigating peptide-mediated molecular recognition. Researchers utilize it to examine binding interactions with nucleic acids, protein surfaces, or membrane components, thereby elucidating the principles governing selective peptide-target associations. These insights are critical for advancing the design of high-affinity ligands, biosensors, and molecular probes in biochemical research.
Peptide synthesis method development: The synthesis of complex cyclic peptides such as this one provides a robust platform for optimizing and validating novel peptide cyclization strategies, coupling chemistries, and purification protocols. Synthetic chemists often employ such molecules to benchmark the efficiency of head-to-tail cyclization, evaluate orthogonal protecting group schemes, and test the scalability of solid-phase peptide synthesis (SPPS) techniques. The challenges presented by incorporating D-amino acids and non-canonical residues further enhance its utility as a reference compound for advancing peptide synthesis methodologies.
Biophysical characterization: The conformational constraints and sequence diversity of this cyclic peptide render it a valuable model for biophysical analysis, including studies of secondary structure, ring strain, and dynamic behavior in solution. Techniques such as nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), and molecular modeling often utilize such peptides to investigate the impact of cyclization and stereochemical inversion on peptide folding and stability. These biophysical insights support the rational engineering of peptides with tailored properties for diverse research applications.
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