Arg-Gly-Asp-Cys is the binding motif of fibronectin to cell adhesion molecules, and can inhibit platelet aggregation and fibrinogen binding.
CAT No: R1213
CAS No:109292-46-8
Synonyms/Alias:H-Arg-Gly-Asp-Cys-OH;Arg-Gly-Asp-Cys;109292-46-8;CHEMBL290071;(3S)-3-[[2-[[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]amino]acetyl]amino]-4-[[(1R)-1-carboxy-2-sulfanylethyl]amino]-4-oxobutanoic acid;(6S,12S,15R)-1,6-diamino-12-(carboxymethyl)-1-imino-15-(mercaptomethyl)-7,10,13-trioxo-2,8,11,14-tetraazahexadecan-16-oic acid;RGDC, R-G-D-C;HY-P0314;BDBM50034704;DA-53838;FA108900;H-Arg-Gly-Asp-Cys-OH trifluoroacetate salt;G77859;(S)-3-[2-((S)-2-Amino-5-guanidino-pentanoylamino)-acetylamino]-N-((R)-1-carboxy-2-mercapto-ethyl)-succinamic acid;
Arg-Gly-Asp-Cys is a synthetic peptide composed of four amino acids—arginine, glycine, aspartic acid, and cysteine—arranged in a specific sequence that imparts unique biochemical properties. This tetrapeptide is notable for containing the Arg-Gly-Asp (RGD) motif, which is well-recognized for its ability to mediate cell adhesion through interactions with integrin receptors. The addition of cysteine at the C-terminus introduces a reactive thiol group, allowing for site-specific conjugation and functionalization. As a result, Arg-Gly-Asp-Cys plays a critical role in cell biology research, biomaterials engineering, and studies focused on extracellular matrix interactions, making it a versatile tool for a range of scientific applications.
Cell Adhesion Studies: The RGD sequence within Arg-Gly-Asp-Cys serves as a high-affinity recognition site for integrin receptors on the cell surface, particularly those involved in the attachment of cells to extracellular matrix proteins such as fibronectin and vitronectin. Researchers utilize this peptide to probe integrin-mediated signaling pathways, dissect mechanisms of cell migration, and evaluate the influence of specific adhesion motifs on cellular behavior. Its defined structure allows for precise interrogation of cell-matrix interactions in both two-dimensional and three-dimensional culture systems.
Surface Functionalization: The terminal cysteine residue provides a reactive thiol group that is highly amenable to covalent coupling strategies, such as maleimide-thiol chemistry. This feature enables site-specific immobilization of the peptide onto a variety of substrates, including gold surfaces, hydrogels, and polymeric scaffolds. Functionalizing biomaterial surfaces with Arg-Gly-Asp-Cys facilitates the creation of bioactive interfaces that promote selective cell attachment and spreading, which is essential for the development of advanced tissue engineering constructs and biosensor platforms.
Peptide Conjugation and Labeling: Due to the presence of the cysteine thiol, this tetrapeptide is frequently employed as a modular building block in the synthesis of peptide conjugates. It can be readily linked to fluorescent dyes, affinity tags, or drug molecules, enabling the generation of multifunctional probes for imaging, affinity purification, or targeted delivery studies. The site-specific nature of the conjugation minimizes structural heterogeneity and preserves the biological activity of the RGD motif, ensuring reliable performance in downstream applications.
Extracellular Matrix Mimicry: In biomaterials research, Arg-Gly-Asp-Cys is incorporated into synthetic matrices to recapitulate the cell-adhesive properties of natural extracellular matrix proteins. By controlling the density and spatial presentation of the peptide within hydrogels or other scaffolding materials, scientists can modulate cell adhesion, proliferation, and differentiation responses. This approach is instrumental in designing in vitro models that more accurately reflect physiological microenvironments, thereby advancing studies in cell biology, regenerative medicine, and tissue morphogenesis.
Integrin Binding Assays: The well-characterized affinity of the RGD motif for integrin receptors makes this peptide a valuable reagent in quantitative binding assays. It is commonly used to assess the specificity and strength of integrin-ligand interactions, screen for integrin inhibitors, and validate the efficacy of surface modifications intended to enhance cell adhesion. These assays provide critical insights into integrin biology and support the rational design of biomaterials with tailored cell-interactive properties.
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