GRGDSP, a synthetic linear RGD peptide, is an integrin inhibitor.
CAT No: R1398
CAS No:91037-75-1
Synonyms/Alias:Grgdsp;H-Gly-Arg-Gly-Asp-Ser-Pro-OH;91037-75-1;GRGDSP TFA;Gly-arg-gly-asp-ser-pro;(2S)-1-[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[(2-aminoacetyl)amino]-5-(diaminomethylideneamino)pentanoyl]amino]acetyl]amino]-3-carboxypropanoyl]amino]-3-hydroxypropanoyl]pyrrolidine-2-carboxylic acid;Glycyl-arginyl-glycyl-aspartyl-seryl-proline;MFCD00076460;CHEMBL6602;Glycyl-L-arginylglycyl-L-aspartyl-L-seryl-L-proline;SCHEMBL2790805;HY-P0290;NCGC00167214-01;DA-53978;FG110187;MS-30494;(2S)-1-[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[(2-aminoacetyl)amino]-5-guanidino-pentanoyl]amino]acetyl]amino]-4-hydroxy-4-oxo-butanoyl]amino]-3-hydroxy-propanoyl]pyrrolidine-2-carboxylic acid;
GRGDSP, known as Gly-Arg-Gly-Asp-Ser-Pro, is a synthetic hexapeptide that incorporates the well-characterized RGD (Arg-Gly-Asp) motif, a critical sequence for cell adhesion processes. As a peptide compound, GRGDSP is widely recognized for its ability to interact with integrin receptors on cell surfaces, mimicking natural extracellular matrix (ECM) proteins such as fibronectin. Its biochemical significance lies in its capacity to modulate cell-matrix interactions, influence cellular signaling pathways, and serve as a functional ligand in diverse experimental systems. Due to its defined sequence and robust activity, GRGDSP is a valuable tool in research focused on cell biology, tissue engineering, and biomaterials development.
Cell Adhesion Studies: GRGDSP is extensively employed in investigating integrin-mediated cell adhesion mechanisms. By presenting the RGD sequence, it facilitates the attachment of various cell types to substrates, enabling precise dissection of integrin-ligand interactions. Researchers utilize the peptide to study cell spreading, migration, and the influence of ECM cues on cellular behavior in vitro. Its defined structure allows for controlled experimentation, aiding in the elucidation of adhesion-dependent signaling pathways and the role of specific integrin subtypes in cellular responses.
Surface Modification and Biomaterials Engineering: The peptide is frequently used to functionalize biomaterial surfaces, including hydrogels, scaffolds, and microcarriers, to enhance biocompatibility and promote cell attachment. Incorporation of GRGDSP into synthetic or natural matrices provides bioactive sites that mimic native ECM components, supporting the development of advanced materials for tissue engineering and regenerative medicine research. Its application enables precise control over cell-material interactions, facilitating studies on cell proliferation, differentiation, and tissue formation within engineered constructs.
Cell Migration and Wound Healing Models: In vitro assays investigating cell migration, such as scratch wound assays or transwell migration systems, often utilize GRGDSP to stimulate integrin-dependent motility. By serving as a chemoattractant or substrate coating, the peptide allows for the assessment of migratory behavior under defined conditions. This approach is instrumental in probing the molecular mechanisms governing cell movement, cytoskeletal dynamics, and the regulatory roles of integrin signaling in processes analogous to wound repair and tissue remodeling.
Integrin Signaling Pathway Analysis: The defined interaction between GRGDSP and integrin receptors makes it a powerful tool for dissecting downstream signaling events. Researchers exploit the peptide to selectively activate or inhibit specific integrin-mediated pathways, providing insights into cellular processes such as survival, proliferation, and gene expression. Its use in biochemical assays, such as immunoprecipitation or phosphorylation studies, enables the characterization of integrin-associated proteins and the mapping of intracellular signaling cascades triggered by ECM engagement.
High-Throughput Screening and Analytical Assays: GRGDSP serves as a reference ligand or competitive inhibitor in various high-throughput platforms designed to screen for integrin-binding molecules or modulators of cell adhesion. Its application in enzyme-linked immunosorbent assays (ELISA), surface plasmon resonance (SPR), and cell-based binding assays supports the identification and characterization of novel compounds with potential to influence integrin function. The peptide's well-defined activity profile ensures reproducibility and reliability in quantitative assays, contributing to the advancement of integrin-targeted research and discovery efforts.
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