c(phg-isoD-G-R-(NMe)k) is a selective α5β1 integrin ligand with an IC50 of 2.9 nM.
CAT No: 10-101-264
CAS No:1844830-65-4
Synonyms/Alias:c(phg-isoDGR-(NMe)k);1844830-65-4;(5S,8R,11R,14S)-8-(4-aminobutyl)-5-[3-(diaminomethylideneamino)propyl]-7-methyl-3,6,9,12,16-pentaoxo-11-phenyl-1,4,7,10,13-pentazacyclohexadecane-14-carboxylic acid;EX-A7488;DA-61970;HY-111413;CS-0040557;
Chemical Name:Cyclo(Arg-NMe-DLys-DPhg-β-Asp-Gly)
c(phg-isoDGR-(NMe)k), also known as a cyclic peptide featuring the isoDGR motif and a methylated lysine residue, represents a sophisticated synthetic carbohydrate compound with unique molecular architecture. The inclusion of the isoDGR sequence, a well-recognized integrin-binding motif, endows this peptide with high specificity for certain integrin subtypes, particularly those implicated in cell adhesion and migration. The cyclic structure imparts enhanced stability and resistance to enzymatic degradation compared to linear analogs, while the methylation of lysine further modulates biological activity and binding affinity. Its design is informed by structural biology and rational drug design principles, making it a valuable tool for researchers delving into cellular signaling, protein-ligand interactions, and biomaterials development. The compound's chemical versatility allows for conjugation with various probes or carriers, expanding its utility across multiple experimental platforms in the life sciences.
Integrin Targeting and Cell Adhesion Studies: c(phg-isoDGR-(NMe)k) serves as a potent integrin ligand for investigating cell adhesion mechanisms. By mimicking natural extracellular matrix sequences, it enables researchers to dissect the roles of specific integrin receptors, such as αvβ3 and α5β1, in mediating cellular attachment, spreading, and migration. When immobilized on culture substrates or incorporated into hydrogels, the peptide can modulate cell behavior, facilitating the study of integrin-dependent signaling pathways and the development of biomimetic materials for tissue engineering research. Its resistance to proteolysis ensures experimental reproducibility and longevity in cell-based assays.
Targeted Delivery Systems: The isoDGR motif within this cyclic peptide is frequently exploited for targeted delivery applications. By conjugating the compound to nanoparticles, liposomes, or other drug carriers, researchers can achieve selective binding to integrin-overexpressing cells, enhancing the specificity and efficiency of payload delivery. This strategy is particularly valuable in the context of imaging agent development or the design of advanced delivery vehicles for research compounds, as it minimizes off-target effects and improves localization to desired cell populations. The modularity of c(phg-isoDGR-(NMe)k) allows for facile chemical modification, supporting the creation of multifunctional delivery platforms.
Molecular Imaging Probes: The structure of c(phg-isoDGR-(NMe)k) lends itself to the development of molecular imaging probes for in vitro and in vivo studies. By attaching fluorescent dyes, radiolabels, or other detectable moieties to the peptide, scientists can visualize integrin expression patterns, monitor cellular uptake, or track the biodistribution of labeled constructs in biological systems. This application is instrumental in basic research, enabling the elucidation of receptor dynamics, tissue localization, and the assessment of ligand-receptor interactions under physiological or pathological conditions.
Biomaterials and Surface Functionalization: Researchers leverage the robust integrin-binding properties of this cyclic peptide to functionalize biomaterial surfaces, such as scaffolds, nanoparticles, or medical devices. By grafting the compound onto material surfaces, it is possible to enhance cell adhesion, promote desired cellular responses, and direct tissue integration in experimental settings. This approach is widely adopted in the design of advanced biomaterials for regenerative medicine, where the modulation of cell-material interactions is crucial for optimizing outcomes in tissue engineering and wound healing studies.
Protein Interaction and Structural Biology Research: c(phg-isoDGR-(NMe)k) is also employed as a molecular probe in protein interaction studies and structural biology. Its defined sequence and stable conformation make it suitable for co-crystallization or binding assays aimed at elucidating the structural basis of integrin-ligand recognition. By providing insight into the molecular determinants of binding specificity and affinity, the peptide supports the rational design of next-generation ligands, inhibitors, or therapeutic candidates for research purposes. The combination of chemical stability, biological relevance, and modularity ensures that c(phg-isoDGR-(NMe)k) remains a valuable asset in the toolkit of scientists exploring integrin biology and carbohydrate-based molecular engineering.
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