integrins

Cilengitide (EMD 121974) is a potent integrin inhibitor for the αvβ3 5 receptor (IC50: 4.1 79 nM, in cell-free assays) with approximately 10-fold selectivity against gpIIbIIIa.

Arg-Gly-Asp-Ser (RGDS peptide) is a conserved tetrapeptide sequence found on fibronectin, fibrinogen α, and von Willebrand factor. It binds to integrins on the cell surface, inhibiting thrombin-induced platelet-fibrinogen interaction.

Arg-Gly-Asp TFA (99896-85-2(free base)) (RGD Trifluoroacetate) is a tripeptide that effectively triggers cell adhesion, addresses certain cell lines and elicits specific cell responses; binds to integrins.

GRGDSPK acetate shows inhibitory activity against integrin-fibronectin binding and can be used in research on integrins in bone formation and resorption.

Arginine-glycine-aspartic acid

GRGDSPK TFA (EMD 56574 TFA) is a peptide containing the Arg-Gly-Asp (RGD) sequence, serving as a competitive and reversible inhibitor of integrin-fibronectin binding. This compound is utilized in research to elucidate integrins' involvement in bone formation and resorption [1] [2].

Certepetide (CEND-1), also known as iRGD, is a bifunctional cyclic peptide that enhances tumor penetration. By interacting with alphav-integrins through its RGD motif and activating NRP-1, it transforms the solid tumor microenvironment into a temporary conduit for therapeutic agents. This property facilitates Certepetide's accumulation in tumors, making it a valuable tool in researching pancreatic cancer and other solid tumors [1] [2] [3].

cRGDfK-thioacetyl ester, a bioactive polypeptide, exhibits selective affinity for integrins and can modify near-infrared (NIR) fluorescent probes for targeted cancer imaging [1] [2].

RGD-Targeted Proapoptotic Peptide is a peptide that preferentially binds to integrins at sites of tumor angiogenesis through its C-terminal RGD-4C sequence (ACDCRGDCFC).

G-{d-Arg}-GDSP, an RGD peptide analogue, binds to the adhesion receptor of integrins, inhibiting cellular attachment to fibronectin and osteoclast resorption [1].

FN-A208 is an active peptide combining A208 from murine laminin a1 with the fibronectin active site GRGDS, linked by a glycine spacer. This compound self-assembles into amyloid-like fibrils and facilitates fibroblast cell adhesion through actin stress fiber formation, suggesting its use as a bioadhesive in tissue regeneration and engineering. FN-A208 targets IKVAV receptors and integrins, but its function can be inhibited by EDTA.

RGD Trifluoroacetate is a tripeptide that effectively triggers cell adhesion, targets specific cell lines, and elicits particular cell responses by binding to integrins. It is the most effective and frequently used peptide sequence for stimulated cell adhesion on synthetic surfaces. Among the 24 integrins that bind to ECM molecules in an RGD-dependent manner are α3β1, α5β1, α8β1, αIIbβ3, αvβ1, αvβ3, αvβ5, αvβ6, αvβ8, and to some extent α2β1 and α4β1.

Fibronectin is a high-molecular weight (~440kDa) extracellular matrix glycoprotein that binds to membrane-spanning receptor proteins called integrins.In addition to integrins, fibronectin also binds extracellular matrix components such as collagen, fibrin