Gly-Arg-Gly-Asp-Ser is a pentapeptide that forms the cell-binding domain of a glycoprotein, osteopontin.
CAT No: R1887
CAS No:96426-21-0
Synonyms/Alias:Gly-arg-gly-asp-ser;96426-21-0;GRGDS;H-Gly-Arg-Gly-Asp-Ser-OH;glycyl-arginyl-glycyl-aspartyl-serine;MFCD00076459;CHEMBL417553;(3S)-3-[[2-[[(2S)-2-[(2-aminoacetyl)amino]-5-(diaminomethylideneamino)pentanoyl]amino]acetyl]amino]-4-[[(1S)-1-carboxy-2-hydroxyethyl]amino]-4-oxobutanoic acid;L-Serine, N-(N-(N-(N2-glycyl-L-arginyl)glycyl)-L-alpha-aspartyl)-;NH2-Gly-Arg-Gly-Asp-Ser;SCHEMBL17440322;DTXSID60914518;HY-P0295;96426-21-0( free base );BDBM50006330;BDBM50414896;H-Gly-Arg-Gly-Asp-Ser-OH TFA salt;NCGC00167212-01;AS-77819;DA-74133;FG108418;Gly-Arg-Gly-Asp-Ser, >=97% (HPLC);G12228;(3S)-3-{2-[(2S)-2-(2-AMINOACETAMIDO)-5-CARBAMIMIDAMIDOPENTANAMIDO]ACETAMIDO}-3-{[(1S)-1-CARBOXY-2-HYDROXYETHYL]CARBAMOYL}PROPANOIC ACID;(6S,12S,15S)-1-amino-6-(2-aminoacetamido)-12-(carboxymethyl)-15-(hydroxymethyl)-1-imino-7,10,13-trioxo-2,8,11,14-tetraazahexadecan-16-oic acid;3-{[2-({2-[(2-Amino-1-hydroxyethylidene)amino]-5-carbamimidamido-1-hydroxypentylidene}amino)-1-hydroxyethylidene]amino}-4-[(1-carboxy-2-hydroxyethyl)imino]-4-hydroxybutanoic acid;3-{2-[2-(2-Amino-acetylamino)-5-guanidino-pentanoylamino]-acetylamino}-N-(1-carboxy-2-hydroxy-ethyl)-succinamic acid;
Chemical Name:(3S)-3-[[2-[[(2S)-2-[(2-aminoacetyl)amino]-5-(diaminomethylideneamino)pentanoyl]amino]acetyl]amino]-4-[[(1S)-1-carboxy-2-hydroxyethyl]amino]-4-oxobutanoic acid
GRGDS (Glycine-Arginine-Glycine-Aspartic acid-Serine) is a synthetic pentapeptide widely recognized for its role as a minimal cell adhesion motif derived from the larger fibronectin protein. As a peptide compound, GRGDS contains the essential Arg-Gly-Asp (RGD) sequence, which is crucial for mediating cell attachment through interactions with integrin receptors on the cell surface. Its biochemical significance stems from its ability to mimic natural extracellular matrix (ECM) signals, making it a powerful tool for probing cell-matrix interactions, modulating cellular behavior, and engineering bioactive surfaces in a variety of research and development settings.
Cell Adhesion Studies: GRGDS is extensively utilized in cell biology research to investigate integrin-mediated cell adhesion mechanisms. By incorporating this peptide into substrates or coatings, researchers can selectively promote or inhibit cellular attachment, spreading, and migration in vitro. The RGD motif's high affinity for integrins such as αvβ3 and α5β1 enables precise dissection of cell-ECM signaling pathways, facilitating studies on cell motility, cytoskeletal organization, and signal transduction.
Tissue Engineering and Biomaterials: In the field of tissue engineering, GRGDS is frequently conjugated to biomaterial scaffolds to enhance cellular compatibility and direct tissue-specific cell responses. The peptide's presence on synthetic matrices or hydrogels supports the attachment and proliferation of anchorage-dependent cells, such as fibroblasts, endothelial cells, and stem cells. By enabling controlled cell-material interactions, GRGDS-functionalized biomaterials contribute to the development of advanced constructs for regenerative medicine, wound healing models, and implantable devices.
Cell Migration and Invasion Assays: The pentapeptide is a valuable reagent in migration and invasion assays, where it serves as a chemoattractant or substrate coating to study directed cell movement. Researchers employ GRGDS to mimic ECM cues in transwell, scratch, or Boyden chamber assays, thereby elucidating the molecular mechanisms underlying processes such as metastasis, angiogenesis, and tissue remodeling. Its defined sequence allows for reproducible experimental conditions and the ability to modulate integrin engagement with high specificity.
Inhibition of Integrin-Mediated Interactions: GRGDS is also applied as a competitive inhibitor to block endogenous RGD-dependent integrin binding in various experimental models. By introducing soluble peptide into cell cultures or in vitro systems, scientists can transiently disrupt cell-ECM interactions, enabling the functional analysis of integrin signaling pathways and the assessment of integrin-specific contributions to cellular processes. This approach is instrumental in delineating the roles of individual integrin subtypes and their downstream signaling cascades.
Surface Functionalization and Biosensor Development: The peptide's well-characterized integrin-binding properties make it a preferred choice for surface modification in biosensor and diagnostic device fabrication. GRGDS can be immobilized on sensor platforms to create bioactive interfaces that selectively capture target cells or proteins expressing RGD-recognizing integrins. Such functionalized surfaces enhance the sensitivity and specificity of cell-based assays, support high-throughput screening applications, and facilitate the development of integrin-targeted analytical technologies.
Through these diverse applications, GRGDS serves as a fundamental tool in the study of cell-matrix interactions, the engineering of bioactive materials, and the advancement of integrin-focused research. Its versatility and molecular precision make it indispensable for scientists seeking to unravel the complexities of cellular adhesion, migration, and signaling within both basic and applied life science disciplines.
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