Cyclo(-Arg-Ala-Asp-D-Phe-Glu) Trifluoroacetate forms a cyclic pentapeptide mimicking RGD-like recognition motifs. The sequence balances charge and hydrophobicity, supporting integrin-binding investigations. Researchers analyze its conformational rigidity and ligand-receptor specificity. Applications include adhesion-motif research, cyclic-peptide engineering, and receptor-binding assays.
CAT No: R2594
CAS No:756500-24-0
Synonyms/Alias:756500-24-0;Cyclo(-Arg-Ala-Asp-D-Phe-Glu) Trifluoroacetate;3-[(2S,5S,8S,11S,14R)-14-benzyl-11-(carboxymethyl)-5-[3-(diaminomethylideneamino)propyl]-8-methyl-3,6,9,12,15-pentaoxo-1,4,7,10,13-pentazacyclopentadec-2-yl]propanoic acid;2,2,2-trifluoroacetic acid;DA-67185;RGD Negative Control trifluoroacetate salt;
Cyclo(-Arg-Ala-Asp-D-Phe-Glu) Trifluoroacetate is a synthetic cyclic pentapeptide distinguished by its stable ring structure and specific sequence of amino acid residues, including both L- and D-amino acids. The incorporation of D-phenylalanine within its backbone enhances resistance to enzymatic degradation, making it a valuable tool in studies requiring prolonged peptide activity. Its unique sequence and conformation are designed to mimic or disrupt protein-protein interactions, particularly those involving integrin receptors, thus offering significant potential in cellular adhesion and signaling research. As a research-use peptide, it is frequently employed in investigations of molecular recognition, receptor binding, and structure-activity relationships within biological systems.
Cell Adhesion Research: Cyclic peptides containing the RGD motif, such as this compound, are extensively utilized to probe integrin-mediated cell adhesion processes. The cyclic nature of the molecule imparts conformational rigidity, enhancing its affinity and selectivity for specific integrin subtypes, including those involved in extracellular matrix interactions. Researchers leverage this property to dissect the molecular mechanisms underlying cell attachment, spreading, and migration, providing insights into fundamental aspects of tissue organization and cellular communication.
Receptor Binding Studies: The defined sequence and conformation of this cyclic pentapeptide make it an effective ligand for studying integrin receptor specificity and binding kinetics. By serving as a competitive inhibitor or molecular probe, it enables detailed characterization of receptor-ligand interactions at the cell surface. Such studies are instrumental in elucidating the structural determinants of integrin recognition and in mapping binding domains critical for downstream signaling events.
Peptide-Protein Interaction Analysis: Due to its structural stability and resistance to proteolytic cleavage, this cyclic peptide is well suited for use in assays investigating peptide-mediated modulation of protein-protein interactions. Its application facilitates the identification of binding partners, mapping of interaction interfaces, and exploration of conformational changes induced by ligand engagement. These insights are crucial for understanding the regulatory roles of peptides in cellular signaling networks.
Surface Functionalization: The robust and well-defined structure of this cyclic pentapeptide allows for its incorporation into biomaterial coatings and surface modification protocols. By immobilizing the peptide on substrates, researchers can create bioactive surfaces that promote or inhibit cell adhesion in a controlled manner. Such functionalized materials are valuable in the development of biosensors, tissue engineering scaffolds, and platforms for cell-based assays, where precise modulation of cell-material interactions is required.
Drug Discovery and Screening: In early-stage drug development, cyclic peptides with RGD motifs serve as important scaffolds for the identification and optimization of integrin-targeting compounds. The unique binding properties and enhanced stability of this molecule enable its use in high-throughput screening assays designed to evaluate the efficacy of novel analogs or small-molecule inhibitors. By providing a reliable benchmark for integrin engagement, it supports the rational design of new therapeutic candidates targeting cell adhesion pathways for research purposes.
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