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| Description | G-{d-Arg}-GDSP (CAS: 111844-21-4) is an RGD peptide analog, sequence Gly-{D-Arg}-Gly-Asp-Ser-Pro with D-arginine at position 2, molecular formula C₂₂H₃₇N₉O₁₀, MW 587.58 Da. It binds integrin adhesion receptors, inhibiting cellular attachment to fibronectin and osteoclast bone resorption; the D-amino-acid modification confers proteolytic stability. It is a tool peptide for studying RGD-integrin interactions, cell-adhesion signaling, and bone-metabolism regulation. |
| Structure type | Linear 6-mer (D-Arg at position 2, RGD analog) |
| Solubility | Readily soluble in water, PBS |
| Storage | Powder -20°C, dry, protected from light |
Product Basic Information Table
| Product Standard English Name | Product Abbreviation / Alias | Function Tags (comma-separated) | Core Structure | Molecular Formula | Exact Mass (Da) | Average MW (Da) | Salt Form | Length (aa) |
| D-Arg-substituted RGD Hexapeptide GDRGDSP (Gly-D-Arg-Gly-Asp-Ser-Pro, protease-resistant, free acid) | GDRGDSP; Gly-D-Arg-Gly-Asp-Ser-Pro; G-DArg-G-D-S-P; D-Arg protease-resistant analog of GRGDSP; D-arginine-substituted RGD peptide; proteolytically stable RGD integrin ligand; free acid; CAS 111844-21-4 | RGD peptide, integrin ligand, αvβ3, α5β1, D-amino acid, protease-resistant, long half-life, cell-adhesion regulation, integrin antagonist, tumor angiogenesis, fibronectin-derived | Linear 6-aa short peptide, sequence Gly-D-Arg-Gly-Asp-Ser-Pro (G-DArg-G-D-S-P); based on the classical fibronectin-derived hexapeptide GRGDSP (Gly-Arg-Gly-Asp-Ser-Pro), with the internal L-Arg at position 2 replaced by D-arginine (D-Arg); side-chain net charge ~0 (D-Arg +1 and Asp −1 cancel; zwitterionic only via the terminal alpha-amino/alpha-carboxyl); retains the intact Arg-Gly-Asp (RGD) core integrin-recognition tripeptide; contains ONE D-configured amino acid (D-Arg) that is NOT recognized/cleaved by common L-specific proteases (trypsin, chymotrypsin, serum/tissue proteases), thereby strongly resisting enzymatic degradation and prolonging half-life in biological systems/serum; D-Arg and L-Arg have identical molecular formula (C22H37N9O10), differing only in stereochemistry; no Cys/Met/Trp (no disulfide, no thiol oxidation, no photo-oxidation); supplied as the free acid; CAS 111844-21-4 | C22H37N9O10 | 587.27 | 587.59 | Free acid; no added counterion; CAS 111844-21-4 | 6 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-GDRGDSP-01 | White to off-white powder | Store at -20°C, sealed, desiccated, protected from light (~2 years). Aliquot to avoid repeated freeze-thaw. No Met/Cys/Trp-low oxidation/photo-oxidation risk; the D-Arg confers intrinsic resistance to proteolysis, so solid stability is excellent. Keep in a desiccator. | 2–8°C for up to ~1 month; working aliquots at -20°C; stable for short shipping at ambient. | Zwitterionic hexapeptide with an RGD core; good water solubility (≥5–10 mg/mL in aqueous buffers). At physiological pH the D-Arg (+1) and Asp (−1) side chains cancel, giving near-neutral charge. Owing to the D-Arg, this peptide is markedly protease-resistant: in serum, enzyme-containing buffers or cell culture it degrades much more slowly than the all-L GRGDSP, making it suitable for integrin-antagonism/cell-adhesion experiments requiring prolonged action. No Cys (no disulfide/thiol oxidation), no Met (no oxidation), no Trp (no photo-oxidation)-good solution stability; wall adsorption is lower than for strongly cationic peptides, though low-binding consumables are still recommended at very low concentrations. | solid stable for ~2 years at -20°C, sealed and desiccated; no oxidizable residues, moderately hygroscopic-keep the desiccator sealed. |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-GDRGDSP-01 | A protease-resistant RGD analog in which the internal Arg of the classical RGD hexapeptide GRGDSP is replaced by D-arginine; it retains RGD integrin-binding activity (αvβ3/αvβ5/α5β1 etc.) while the D-amino acid evades common proteases, markedly prolonging half-life in biological systems-used for long-acting integrin antagonism, cell-adhesion regulation and peptide-drug design. | This is the D-arginine-substituted analog GDRGDSP (Gly-D-Arg-Gly-Asp-Ser-Pro) of the classical fibronectin-derived RGD hexapeptide GRGDSP (Gly-Arg-Gly-Asp-Ser-Pro). The Arg-Gly-Asp (RGD) tripeptide is the minimal, most canonical recognition motif of the integrin family: it competitively occupies the ligand-binding pocket of αvβ3 (vitronectin receptor), αvβ5, α5β1 (fibronectin receptor) and αIIbβ3 (platelet fibrinogen receptor), blocking engagement of ECM ligands such as fibronectin, vitronectin, fibrinogen and osteopontin, and thereby regulating integrin-mediated cell adhesion, spreading, migration, survival and angiogenesis. The native all-L RGD hexapeptide has a very short circulatory half-life in vivo (often minutes to tens of minutes) due to rapid serum proteolysis-the main bottleneck for linear RGD peptides in drug/imaging research. By replacing the internal Arg with D-arginine, this site no longer is recognized and cleaved by L-specific proteases (e.g., trypsin cleavage at Arg), so the peptide retains RGD integrin-binding activity while gaining markedly improved serum/in-vivo stability and prolonged action-a standard enzyme-stabilization strategy in the design of long-acting integrin antagonists and RGD-targeting peptides (e.g., for tumor neovasculature αvβ3 imaging/therapy) and anti-adhesion peptide drugs. D-Arg and L-Arg share the same molecular formula; GDRGDSP is identical in formula/MW to all-L GRGDSP (C22H37N9O10), differing only in stereochemistry. No Cys/Met/Trp, so both solid and solution stability are good. | Integrin biology, RGD peptide-drug design, tumor neovasculature/αvβ3 targeting, anti-angiogenesis, cell-adhesion and migration control, anti-metastasis research, cardiovascular implant endothelialization, anti-platelet/thrombosis research, enzyme-stabilized peptide engineering (D-amino-acid strategy) | Integrins αvβ3 (vitronectin receptor), αvβ5, α5β1 (fibronectin receptor), αIIbβ3 (platelet GPIIb/IIIa); competitive antagonism of ECM ligands (fibronectin, vitronectin, fibrinogen, osteopontin); the D-Arg site resists trypsin/serum-protease hydrolysis |
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