RGDS is a classic adhesion motif interacting with integrin receptors and influencing cell-matrix communication. The short sequence promotes studies of β-turn formation, surface binding, and ligand-receptor docking. Researchers use it to probe extracellular-matrix interactions and receptor specificity. Its simplicity supports widespread biochemical and structural analyses.
CAT No: R1883
CAS No:91037-65-9
Synonyms/Alias:Arg-gly-asp-ser;91037-65-9;Rgds peptide;Fibronectin tetrapeptide;Arginyl-glycyl-aspartyl-serine;RGDS;UNII-AC6UDA2MFC;L-Arginylglycyl-L-alpha-aspartyl-L-serine;AC6UDA2MFC;MFCD00076452;CHEMBL265628;(3S)-3-[[2-[[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]amino]acetyl]amino]-4-[[(1S)-1-carboxy-2-hydroxyethyl]amino]-4-oxobutanoic acid;L-Serine, N-(N-(N-L-arginylglycyl)-L-alpha-aspartyl)-;RGDS peptide; Fibronectin tetrapeptide;Arg-Gly-Asp-Ser?;Fibronectin Inhibitor;Arg-Gly-Asp-Ser peptide;H-Arg-Gly-Asp-Ser-OH;L-Serine, L-arginylglycyl-L-alpha-aspartyl-;SCHEMBL7394659;DTXSID50920002;Fibronectin Inhibitor Tetrapeptide;CHEBI:232857;NNRFRJQMBSBXGO-CIUDSAMLSA-N;BDBM50241180;DU-728;RGDS peptide;Fibronectin tetrapeptide;AKOS024457642;Arg-Gly-Asp-Ser, >=95% (HPLC);CS-3266;FR73590;NCGC00167153-01;(6S,12S,15S)-1,6-diamino-12-(carboxymethyl)-15-(hydroxymethyl)-1-imino-7,10,13-trioxo-2,8,11,14-tetraazahexadecan-16-oic acid;AS-56630;DA-61200;HY-12290;C77102;BRD-K08859203-001-01-9;L-SERINE, L-ARGINYLGLYCYL-L-.ALPHA.-ASPARTYL-;Q27273860;(3S)-3-{2-[(2S)-2-AMINO-5-CARBAMIMIDAMIDOPENTANAMIDO]ACETAMIDO}-3-{[(1S)-1-CARBOXY-2-HYDROXYETHYL]CARBAMOYL}PROPANOIC ACID;(6S,12S,15S)-1,6-diamino-12-(carboxymethyl)-16-hydroxy-1-imino-7,10,13-trioxo-2,8,11,14-tetraazahexadecane-15-carboxylic acid;(S)-3-[2-((S)-2-Amino-5-guanidino-pentanoylamino)-acetylamino]-N-((R)-1-carboxy-2-hydroxy-ethyl)-succinamic acid;(S)-3-[2-((S)-2-Amino-5-guanidino-pentanoylamino)-acetylamino]-N-((S)-1-carboxy-2-hydroxy-ethyl)-succinamic acid;2-[1-[1-amino-4-amino(imino)methylamino-(1S)-butylcarboxamidomethylcarboxamido]-2-carboxy-(1S)-ethylcarboxamido]-3-hydroxy-(2S)-propanoic acid;2-{1-[1-amino-4-amino(imino)methylaminobutylcarboxamidomethylcarboxamido]-2-carboxyethylcarboxamido}-3-hydroxypropanoic acid;3-({2-[(2-Amino-5-carbamimidamido-1-hydroxypentylidene)amino]-1-hydroxyethylidene}amino)-4-[(1-carboxy-2-hydroxyethyl)imino]-4-hydroxybutanoic acid;3-[(S)-2-((S)-2-Amino-5-guanidino-pentanoylamino)-acetylamino]-N-(1-carboxy-2-hydroxy-ethyl)-succinamic acid;3-[2-((S)-2-Amino-5-guanidino-pentanoylamino)-acetylamino]-N-((S)-1-carboxy-2-hydroxy-ethyl)-succinamic acid;3-[2-(2-Amino-5-guanidino-pentanoylamino)-acetylamino]-N-(1-carboxy-2-hydroxy-ethyl)-succinamic acid;3-[2-(2-Amino-5-guanidino-pentanoylamino)-acetylamino]-N-(1-carboxy-2-hydroxy-ethyl)-succinamic acid (RGDS);
Chemical Name:(3S)-3-[[2-[[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]amino]acetyl]amino]-4-[[(1S)-1-carboxy-2-hydroxyethyl]amino]-4-oxobutanoic acid
RGDS, also known as the Arg-Gly-Asp-Ser peptide, is a synthetic tetrapeptide that plays a pivotal role in the study of cell adhesion, extracellular matrix interactions, and integrin-mediated signaling. As a bioactive motif derived from the primary structure of fibronectin and other adhesive proteins, RGDS is widely recognized for its ability to modulate cellular attachment and migration by specifically binding to integrin receptors. This peptide's well-characterized sequence and defined biological activity have established it as a fundamental tool in biochemical, cell biological, and biomaterials research, where precise control of cell-substrate interactions is critical for experimental and translational applications.
Cell Adhesion Studies: RGDS is extensively utilized in investigations of cell adhesion mechanisms due to its high affinity for integrins, particularly those of the αv and β1 subfamilies. By presenting the peptide on culture surfaces or within hydrogels, researchers can selectively stimulate or inhibit integrin-mediated attachment, enabling detailed analysis of cell-matrix interactions, focal adhesion formation, and downstream signaling pathways. This approach facilitates the dissection of molecular mechanisms underlying cellular adhesion, spreading, and migration, providing valuable insights into developmental biology, tissue engineering, and cancer metastasis.
Biomaterials Functionalization: The peptide is frequently employed to functionalize biomaterial surfaces, including polymers, hydrogels, and scaffolds, to enhance cellular compatibility and direct specific cell responses. By covalently linking RGDS to synthetic matrices, scientists can mimic natural extracellular matrix cues, promoting selective cell adhesion and proliferation in engineered tissues. Such functionalization strategies are central to the design of advanced biomaterials for regenerative medicine, implantable devices, and three-dimensional cell culture systems, where controlled bioactivity is essential for successful integration and performance.
Cell Migration and Wound Healing Models: RGDS serves as a critical modulator in in vitro models of cell migration and wound healing. By introducing the peptide into assay systems, investigators can manipulate integrin engagement to study the dynamics of cell movement, chemotaxis, and collective migration. This application is particularly valuable in elucidating the roles of integrin signaling in tissue remodeling, angiogenesis, and the cellular response to injury, supporting the development of new hypotheses regarding the regulation of migratory behaviors in diverse cell types.
Signal Transduction Research: The interaction of RGDS with integrin receptors initiates a cascade of intracellular signaling events that regulate cytoskeletal organization, gene expression, and cell survival. Researchers employ the peptide to selectively activate or block integrin-mediated pathways, enabling the study of downstream effectors such as focal adhesion kinase, MAP kinases, and Rho GTPases. This targeted approach provides a robust platform for dissecting the complexities of cell signaling networks, facilitating the identification of novel regulatory nodes and potential intervention points in cell biology and pathophysiology.
Peptide-Receptor Binding Assays: RGDS is a valuable reagent in quantitative binding assays designed to characterize the specificity and affinity of integrin-ligand interactions. By using labeled or immobilized forms of the peptide, scientists can evaluate the binding kinetics of various integrin subtypes, screen for inhibitors, or assess the competitive effects of other extracellular matrix components. Such assays are instrumental in advancing the understanding of receptor-ligand dynamics, supporting the development of integrin-targeted probes, and informing the rational design of biomimetic materials and inhibitors for research use.
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