gly-arg-gly-asp-ser

Gly-Arg-Gly-Asp-Ser (GRGDS) GRGDS is a cell binding protein domain derived from the cell-binding region of fibronectin.

FITC-Ahx-Gly-Arg-Gly-Asp-Ser-Pro, also known as FITC-linked GRGDSP, is a fluorescent peptide with integrin inhibitory properties, which impedes tumor cell adherence to endothelial blood vessel cells, potentially restricting metastasis [1].

Cyclo(Gly-Arg-Gly-Asp-Ser-Pro) (c(GRGDSP)) is an RGD-containing inhibitory peptide and synthetic α5β1 integrin ligand that competitively inhibits the binding of invasin (Inv) to α5β1 integrin on Caco-2 cells [1].

Gly-Arg-Gly-Asp-Ser (GRGDS) acetate is a cell binding protein domain derived from the cell-binding region of fibronectin.

Gly-Arg-Gly-Asp-Ser (GRGDS) is a cell binding protein domain derived from the cell-binding region of fibronectin. Osteopontin uses this motif for cell adhesion.

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-Ser acetate is an integrin binding sequence that directly and specifically bind pro-caspase-8, pro-caspase-9 and pro-caspase-3, while it does not bind pro-caspase-1. Arg-Gly-Asp-Ser acetate inhibits integrin receptor function.

Arg-Gly-Asp-Ser (TFA) is an integrin-binding sequence that inhibits integrin receptor function by specifically and directly binding to pro-caspase-8, pro-caspase-9, and pro-caspase-3, without interacting with pro-caspase-1 [1].

Cys-Arg-Gly-Asp-Phe-Pro-Ala-Ser-Ser-Cys (Disulfide bridge: Cys1-Cys10), a decapeptide with a cyclic RGD active sequence, functions as an Integrin αIIbβ3 antagonist, effectively inhibiting platelet adhesion and proMMP-13 adhesion [1].

Cys-Asp-Pro-Gly-Tyr-Ile-Gly-Ser-Arg-NH2 is a linear peptide derived from the laminin B1 chain, disrupting tumor cell adherence and invasion into the basement membrane and exhibiting anti-angiogenic properties [1].

SDGR, a tetrapeptide comprising a serine-aspartic acid-glycine-arginine (Ser-Asp-Gly-Arg) sequence, efficiently impedes cell attachment mediated by fibronectin [1].

[Leu144,Arg147]-PLP (139-151) is a mutated fragment of the myelin proteolipid protein (PLP), featuring substitutions of tryptophan to leucine and histidine to arginine at positions 144 and 147, respectively. Immunizing mice with this peptide (50 µg) mixed in complete Freund's adjuvant (CFA) elevates IL-4 levels in the spleen. While it suppresses Th1 cell activation in vitro, it does not do so in vivo; instead, it promotes the development of regulatory T cells. Preimmunization with [Leu144, Arg147]-PLP (139-151) postpones the onset of experimental autoimmune encephalomyelitis (EAE) triggered by encephalitogenic peptides from PLP (178-191), myelin oligodendrocyte glycoprotein (MOG) (92-106), or myelin basic protein (MBP) in mice.

Myelin Basic Protein (MBP) (68-82), guinea pig, is a peptide with the sequence Tyr-Gly-Ser-Leu-Pro-Gln-Lys-Ser-Gln-Arg-Ser-Gln-Asp-Glu-Asn and represents a fragment of myelin basic protein (MBP).

Gly-Arg-Gly-Asp-Ser-Pro (GRGDSP) is used as a soluble integrin-blocking RGD-based peptide.

Peptide 78 is identical to peptide 74 except that serine replaces cysteine. It does not inhibit 72-kDa type IV collagenase.