RGD peptide (GRGDNP) acts as an inhibitor of integrin-ligand interactions and plays an important role in cell adhesion, migration, growth, and differentiation. RGD peptide (GRGDNP) promote apoptosis through activation of conformation changes that enhance pro-caspase-3 activation and autoprocessing.
CAT No: R1657
CAS No:114681-65-1
Synonyms/Alias:114681-65-1;GRGDNP;GLY-ARG-GLY-ASP-ASN-PRO;H-Gly-Arg-Gly-Asp-Asn-Pro-OH;RGD peptide (GRGDNP);CHEMBL2418222;(2S)-1-[(2S)-4-amino-2-[[(2S)-2-[[2-[[(2S)-2-[(2-aminoacetyl)amino]-5-(diaminomethylideneamino)pentanoyl]amino]acetyl]amino]-3-carboxypropanoyl]amino]-4-oxobutanoyl]pyrrolidine-2-carboxylic acid;MFCD00153556;HY-P1740;BDBM50439682;s4513;DA-74132;FG108909;CS-0095103;G12418;(S)-1-((6S,12S,15S)-1-Amino-15-(2-amino-2-oxoethyl)-6-(2-aminoacetamido)-12-(carboxymethyl)-1-imino-7,10,13-trioxo-2,8,11,14-tetraazahexadecan-16-oyl)pyrrolidine-2-carboxylic acid;(S)-1-((6S,12S,15S)-1-amino-15-(2-amino-2-oxoethyl)-6-(2-aminoacetamido)-12-(carboxymethyl)-1-imino-7,10,13-trioxo-2,8,11,14-tetraazahexadecane)pyrrolidine-2-carboxylic acid;
RGD peptide GRGDNP is a synthetic peptide characterized by the presence of the arginine-glycine-aspartic acid (RGD) motif, a sequence recognized for its pivotal role in mediating cell adhesion through integrin binding. As a member of the peptide compound category, GRGDNP is widely utilized in cell biology, biomaterials research, and molecular biology due to its ability to mimic natural extracellular matrix (ECM) ligands. The inclusion of the asparagine-proline (NP) extension in this peptide enhances its solubility and structural stability, making it a valuable tool for probing integrin-mediated cellular processes. Its defined sequence allows for reproducible and specific modulation of cell-surface interactions, supporting advanced studies in cell signaling, tissue engineering, and related fields.
Cell adhesion studies: GRGDNP is extensively employed to investigate integrin-mediated cell adhesion mechanisms. By presenting the RGD motif to cultured cells, researchers can selectively engage integrin receptors such as αvβ3 and α5β1, which are central to cell attachment, migration, and spreading. This peptide enables controlled experiments to dissect the contribution of specific integrins to cellular responses, facilitating the analysis of adhesion-dependent signaling pathways and cytoskeletal rearrangements.
Surface functionalization: In biomaterials science, the peptide serves as a functionalization agent to enhance the bioactivity of various substrates, including hydrogels, polymers, and implant surfaces. Covalent or non-covalent immobilization of GRGDNP onto material surfaces promotes cellular recognition and attachment, thereby improving the integration of synthetic scaffolds with biological tissues. This application is crucial for optimizing the design of tissue engineering constructs and medical device coatings, where controlled cell-material interactions are required.
Cell migration and wound healing assays: The peptide is a key component in in vitro assays that model cell migration, such as scratch wound assays or transwell migration studies. By modulating the local presentation of the RGD motif, GRGDNP allows researchers to assess how integrin engagement influences cell motility, directionality, and invasion. Such assays are fundamental for understanding the molecular basis of tissue regeneration, angiogenesis, and metastatic behavior in various cell types.
Signal transduction research: GRGDNP provides a defined ligand for probing downstream signaling events initiated by integrin activation. Its use in cell culture systems enables the study of pathways such as focal adhesion kinase (FAK), Src family kinases, and other intracellular effectors that regulate proliferation, survival, and differentiation. By comparing cellular responses to RGD-containing peptides versus control sequences, investigators can clarify the specific signaling cascades triggered by integrin engagement.
Competitive inhibition assays: The peptide is frequently utilized as a competitive inhibitor to block natural RGD-mediated interactions between cells and ECM proteins like fibronectin, vitronectin, and laminin. By saturating integrin receptors with GRGDNP, researchers can selectively disrupt endogenous ligand binding, providing a powerful approach to delineate the functional roles of individual integrins in complex biological processes. This strategy is particularly valuable for validating target specificity in drug discovery or for elucidating mechanistic aspects of cell-ECM communication.
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