GRGDSPC, a 7-amino acid peptide, is a thiolated cell adhesion peptide.
CAT No: R1400
CAS No:91575-26-7
Synonyms/Alias:GRGDSPC;91575-26-7;3-[[2-[[2-[(2-aminoacetyl)amino]-5-(diaminomethylideneamino)pentanoyl]amino]acetyl]amino]-4-[[1-[2-[(1-carboxy-2-sulfanylethyl)carbamoyl]pyrrolidin-1-yl]-3-hydroxy-1-oxopropan-2-yl]amino]-4-oxobutanoic acid;L-Cysteine, glycyl-L-arginylglycyl-L-alpha-aspartyl-L-seryl-L-prolyl-, bimol. (7-->7')-disulfide;(glycyl-arginyl-glycyl-aspartyl)-seryl-prolyl-cysteinyl;SCHEMBL2317887;RGD-3506-PI;BFA64679;FG110018;H-Gly-Arg-Gly-Asp-Ser-Pro-Cys-OH trifluoroacetate salt;
GRGDSPC is a synthetic peptide composed of the amino acid sequence Gly-Arg-Gly-Asp-Ser-Pro-Cys. As an RGD-containing peptide, it is widely recognized for its ability to mimic cell adhesion motifs found in extracellular matrix proteins such as fibronectin. The presence of the RGD tripeptide sequence confers high affinity for integrin receptors, making GRGDSPC a valuable tool in studies of cell-matrix interactions, tissue engineering, and biomaterials science. Its terminal cysteine residue allows for facile conjugation to various surfaces or molecules, expanding its versatility in experimental design and functionalization strategies.
Cell adhesion studies: The peptide is extensively utilized as a model ligand for investigating integrin-mediated cell adhesion. By presenting the RGD motif in a defined sequence context, it enables researchers to dissect the molecular mechanisms underlying cell attachment, spreading, and migration on biomimetic surfaces. GRGDSPC's specificity for integrin receptors, particularly those in the αv and β3 families, facilitates the analysis of integrin-subtype selectivity and downstream signaling events, providing critical insights into cell-extracellular matrix communication.
Surface modification and biomaterials engineering: The terminal cysteine in GRGDSPC allows for site-specific attachment to gold, glass, or polymeric substrates via thiol-based chemistries. This property is exploited in the functionalization of biomaterial surfaces to promote cellular interaction and biocompatibility. By immobilizing the peptide onto scaffolds, hydrogels, or medical device coatings, researchers can systematically evaluate how controlled presentation of adhesion ligands influences cell behavior, tissue integration, and material performance in vitro.
Tissue engineering and regenerative medicine research: The sequence is commonly incorporated into three-dimensional scaffolds and hydrogels to mimic the native extracellular matrix environment. Its integrin-binding capability supports the attachment, proliferation, and differentiation of various cell types, including stem cells and primary tissue cells. The use of GRGDSPC in engineered matrices helps elucidate the role of cell-adhesive cues in tissue morphogenesis, regeneration, and repair processes under defined experimental conditions.
Biosensor and assay development: The peptide serves as a functional probe in the design of biosensors and cell-based assays that monitor integrin activity, cell adhesion strength, or ligand-receptor interactions. By immobilizing GRGDSPC on sensor surfaces, researchers can develop quantitative assays for high-throughput screening of integrin antagonists, cell-matrix interaction modulators, or other bioactive compounds. Its defined structure and binding properties ensure reproducible assay performance and facilitate the interpretation of experimental outcomes.
Protein engineering and ligand presentation studies: GRGDSPC is frequently used as a modular building block for the rational design of multifunctional proteins, peptide-polymer conjugates, or nanostructured materials. The sequence can be incorporated into recombinant fusion proteins or synthetic constructs to endow them with integrin-targeting functionality. Through such engineering approaches, scientists can systematically investigate the spatial arrangement, density, and multivalency effects of adhesion ligands on biological responses, advancing the understanding of cell-material interactions at the molecular level.
1. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis
4. The spatiotemporal control of signalling and trafficking of the GLP-1R
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