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 that has garnered significant attention in the field of biochemical research due to its unique sequence and conformational stability. Featuring the amino acids glycine, arginine, aspartic acid, serine, and proline arranged in a specific cyclic structure, this compound exhibits enhanced resistance to enzymatic degradation and improved binding affinity compared to its linear counterparts. The presence of the RGD motif within its sequence is particularly noteworthy, as it is widely recognized for its role in mediating cell adhesion processes. The trifluoroacetate salt form contributes to its solubility and ease of handling, making it a preferred choice for various laboratory applications. Researchers value its versatility and reliability in experimental protocols, particularly those investigating cellular interactions and extracellular matrix dynamics.
Cell Adhesion Studies: Cyclo(-Gly-Arg-Gly-Asp-Ser-Pro) Trifluoroacetate is extensively utilized in cell adhesion assays to investigate the interactions between cells and the extracellular matrix. The cyclic RGD sequence within the peptide enables it to mimic natural ligands for integrin receptors, facilitating the study of integrin-mediated signaling pathways. By coating culture substrates with this peptide, scientists can selectively promote or inhibit the attachment of specific cell types, allowing for the dissection of adhesion mechanisms and the identification of integrin subtypes involved in various physiological and pathological processes. This application is crucial for understanding tissue development, wound healing, and metastasis at the molecular level.
Tissue Engineering Research: The cyclic peptide serves as a valuable tool in tissue engineering, where it is incorporated into biomaterial scaffolds to enhance cellular attachment and proliferation. Its ability to engage integrin receptors promotes the integration of engineered tissues with host environments, supporting the formation of functional tissue constructs. By modifying scaffold surfaces with Cyclo(-Gly-Arg-Gly-Asp-Ser-Pro) Trifluoroacetate, researchers can modulate cell behavior, direct differentiation, and improve the mechanical properties of engineered tissues. This approach is instrumental in the development of advanced biomaterials for regenerative medicine and the repair of damaged tissues, offering insights into scaffold design and functionalization strategies.
Angiogenesis Assays: In the context of angiogenesis research, the cyclic hexapeptide is employed to study the regulation of new blood vessel formation. Through its interaction with endothelial cell integrins, it can either stimulate or inhibit angiogenic responses, depending on the experimental setup. Scientists use this property to elucidate the molecular mechanisms governing vascular development and to screen for potential modulators of angiogenesis. The precise control offered by the peptide's cyclic structure allows for reproducible and reliable results in in vitro and in vivo models, advancing our understanding of vascular biology and its implications in health and disease.
Receptor-Ligand Interaction Analysis: Cyclo(-Gly-Arg-Gly-Asp-Ser-Pro) Trifluoroacetate is frequently applied in studies focused on receptor-ligand interactions, particularly those involving integrins. By serving as a model ligand, it enables the quantitative assessment of binding affinities, receptor specificity, and downstream signaling events. Techniques such as surface plasmon resonance, fluorescence labeling, and competitive binding assays benefit from the stability and defined structure of this peptide. These studies contribute to the rational design of integrin-targeted molecules and the development of novel therapeutic strategies that modulate cell-matrix interactions.
Drug Delivery System Development: The cyclic peptide is explored in the design of targeted drug delivery systems, where its integrin-binding properties are harnessed to achieve selective delivery of therapeutic agents to specific cell types. By conjugating drugs, nanoparticles, or imaging agents to Cyclo(-Gly-Arg-Gly-Asp-Ser-Pro) Trifluoroacetate, researchers can enhance cellular uptake and improve the localization of treatments. This strategy aims to increase efficacy while minimizing off-target effects, and is particularly relevant in the context of targeted therapies and diagnostic imaging. The use of this peptide in drug delivery research highlights its potential to bridge the gap between molecular recognition and practical biomedical applications, driving innovation in the field of precision medicine.
3. The spatiotemporal control of signalling and trafficking of the GLP-1R
4. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
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