Cyclo(-Gly-Arg-Gly-Asp-Ser-Pro) Trifluoroacetate forms a stable cyclic peptide enriched with charged and polar residues. The ring constraint enhances resistance to conformational drift and aids binding-site modeling. Researchers study its interaction geometry and rigidity in solution. Use spans biomaterial design, adhesion-motif analysis, and structural optimization.
CAT No: R2649
CAS No:135432-37-0
Synonyms/Alias:135432-37-0;Cyclo(-Gly-Arg-Gly-Asp-Ser-Pro) Trifluoroacetate;DA-72465;Cyclo(-Gly-Arg-Gly-Asp-Ser-Pro) trifluoroacetate salt;2-[(3S,6S,12S,18S)-12-[3-(diaminomethylideneamino)propyl]-3-(hydroxymethyl)-2,5,8,11,14,17-hexaoxo-1,4,7,10,13,16-hexazabicyclo[16.3.0]henicosan-6-yl]acetic acid;2,2,2-trifluoroacetic acid;
Cyclo(-Gly-Arg-Gly-Asp-Ser-Pro) Trifluoroacetate is a synthetic cyclic hexapeptide featuring the amino acid sequence Gly-Arg-Gly-Asp-Ser-Pro, cyclized to enhance structural stability and functional specificity. Characterized by the presence of the RGD motif, this compound is notable for its strong affinity for integrin receptors, which play critical roles in cell adhesion, signaling, and migration. The incorporation of trifluoroacetate as a counterion aids in peptide solubility and handling, making this molecule a valuable tool in the study of extracellular matrix interactions and receptor-ligand dynamics. Its unique cyclic conformation confers resistance to proteolytic degradation, supporting its use in prolonged or demanding biochemical assays. As such, cyclo(-Gly-Arg-Gly-Asp-Ser-Pro) Trifluoroacetate is widely recognized for its utility in integrin-related research, biomaterials development, and cell biology investigations.
Integrin binding studies: The cyclic peptide is extensively utilized as a selective ligand for integrin subtypes, particularly those recognizing the RGD sequence, such as αvβ3 and α5β1. Its conformational rigidity and enhanced receptor affinity enable precise probing of cell surface integrins, facilitating the elucidation of integrin-mediated signaling pathways. Researchers employ this molecule in receptor binding assays to quantify integrin expression, characterize ligand specificity, and dissect downstream cellular responses triggered by integrin engagement.
Cell adhesion assays: Due to its high affinity for integrins, the peptide serves as a potent modulator of cell adhesion to extracellular matrix components. It is commonly used to coat culture surfaces or as a soluble competitor in adhesion inhibition assays, allowing scientists to analyze the contribution of RGD-mediated interactions to cell attachment, spreading, and migration. These applications are particularly relevant in studies of cancer metastasis, tissue engineering, and wound healing, where integrin-dependent adhesion is a key regulatory factor.
Biomaterials functionalization: The cyclic RGD peptide is frequently incorporated into biomaterial surfaces, hydrogels, or scaffolds to promote cell attachment and modulate cellular responses in vitro and in vivo. Its integration into synthetic matrices enhances biocompatibility and supports the design of advanced tissue engineering constructs. By presenting a biologically active ligand in a protease-resistant format, the peptide enables long-term studies of cell-material interactions and facilitates the development of targeted delivery systems.
Signal transduction research: Owing to its ability to engage integrins and initiate downstream signaling cascades, the peptide is a powerful tool for dissecting pathways involved in cell survival, proliferation, and differentiation. In experimental models, it is applied to stimulate or inhibit specific signaling routes, enabling the investigation of integrin-dependent effects on gene expression, cytoskeletal organization, and cellular phenotype. Such studies contribute to a deeper understanding of how extracellular cues regulate fundamental biological processes.
Competitive inhibition assays: The cyclic peptide is also valuable in competitive binding experiments designed to block endogenous ligand interactions with integrin receptors. By serving as a competitive antagonist, it allows researchers to isolate the functional consequences of integrin blockade, distinguish between integrin-dependent and -independent mechanisms, and validate the specificity of novel integrin-targeted compounds. This approach is instrumental in basic research on cell-matrix interactions as well as in the preclinical evaluation of integrin-modulating agents.
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