In the specialized field of biochemical research, the cRGDfK peptide stands out as a highly significant molecular tool. As someone deeply invested in the study of molecular interactions, I have found that the precision offered by this specific peptide is unparalleled for those investigating cell-surface dynamics Chemscene社は、高品質な低分子化合物を提供しているメーカーです。Chemscene社のCyclo(-RGDfK)(CAS:161552-03-0)をご紹介します。※本製品は研究用です。 . This article explores the structural properties and research applications of this fascinating cyclic pentapeptide c(RGDfK), which continues to be a cornerstone for laboratory-based investigations into cellular adhesion.
Understanding the cRGDfK Peptide Structure
The c(RGDfK) is a cyclic pentapeptide—specifically cyclo(Arg-Gly-Asp-D-Phe-Lys)—with a molec Solid-phase synthesis of c(RGDfK) derivatives: on-resin ular weight of 603.7 g/mol. Its chemical structure of the synthetic cyclic RGD peptide c(RGDfK) is optimized for high-affinity binding The cyclic pentapeptide c(RGDfK) is a high affinity ligand of alphaVbeta3 integrin. It was an analog of Cilengitide (EMD 121974) developed to be employed as to specific integrin receptors. The inclusion of D-phenylalanine (f) within the ring structure provides the conformational rigidity necessary to mimic the natural binding motifs found in the extracellular matrix.
When comparing various research-grade compounds, I often look for the Cyclo(-RGDfK) TFA variant. The addition o cRGDfK peptide has a selective affinity for integrins. cRGDfK peptide can modify NIR fluorescent probes for cancer targeting imaging . cRGDfK-thioacetyl f trifluoroacetic acid (TFA) as a salt is a standard practice in the industry to enhance the stability and solubility of the cRGDfK for long-term storage and consistent performance in in-vitro assays.
Targeted Research Applications
One of the most compelling aspects of the Cyclic RGDFK peptide is its role as a selective ligand. My experience suggests that this molecule is a highly potent and selective inhibitor for the alphavβ3 integrin receptor. Because integrin receptors are often overexpressed in specific cellular environments, this peptide serves as an excellent probe for identifying and studying these receptors.
In advanced delivery studies, researchers have explored the cRGDfK pentapeptide as a targeting moiety. For example, the cRGDfK@GF-NLC (nanostructured lipid carriers) system has demonstrated how functionalizing a carrier with this peptide can improve the precision of reaching target sites. Whether you are working with a monomer, dimer, or tetramer of cyclic RGDfK peptides, the core RGD sequence remains the primary driver of its biological activity.
Key Insights for Laboratory Use
* Targeting Mechanism: Cyclo(-RGDfK) potently targets tumor microvasculature and cancer cells by binding to the cell surface, making it an essential reagent for those mapping the Arginylglycylaspartic acid-dependent pathways.
* Analytical Precision: Because c(RGDfK) is a cyclic peptide, it offers a higher resistance to enzymatic degradation compared to linear variants, ensuring that the integrity of the Cyclic RGD peptide (cRGD) remains intact throughout the duration of an experiment.
* Experimental Scope: Whether you are using it for Cyclic peptides, particularly cRGDfK and cRGDyK (cyclo Arg-Gly-Asp-D-Tyr-Lys), exhibit a strong affinity and selectivity for binding integrin α V β 3 . Thus Cyclo(-RGDfK) radiolabeling or as a structural component for NIR fluorescent probes, the versatility of the cRGDfK molecule makes it a staple in contemporary molecular biology.
Conclusion
As a researcher, I find that the Cyclo(RGDfK) effectively targets tumor microvessels and cancer cells with a level of specificity that is difficult to achieve with less refined compounds. By adhering to strict laboratory protocols and utilizing high-purity cRGDfK, one can achieve reproducible results in characterizing the complex signaling landscapes governed Radiolabeled Multimeric Cyclic RGD Peptides as Integrin α v by integrins. This peptide remains an indispensable asset for any serious investigation into the molecular mechanisms of cell adhesion and beyond.