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| Description | Cys(Npys)-(D-Arg)9 is a 10-amino-acid cell-penetrating peptide with the sequence Cys(Npys)-D-Arg-D-Arg-D-Arg-D-Arg-D-Arg-D-Arg-D-Arg-D-Arg-D-Arg-NH₂ (C(Npys)-(D-Arg)9-NH₂), with an N-terminal 3-nitro-2-pyridinesulfenyl (Npys)-activated cysteine, 9 consecutive D-arginines (D-Arg) in the middle, and C-terminal amidation. This peptide is a D-amino acid and Npys-activated derivative of the classic polyarginine cell-penetrating peptide ((Arg)9). The key advantage of using D-arginine (D-Arg) instead of L-arginine (L-Arg) is that peptides composed of D-amino acids are highly resistant to proteases (such as trypsin, chymotrypsin, aminopeptidases, carboxypeptidases, etc.), because proteases generally can only recognize and cleave peptide bonds composed of L-amino acids. This makes (D-Arg)9 more stable and have a longer half-life in vivo and in serum-containing cell culture media, thereby improving cell penetration and drug delivery efficiency. Nine consecutive D-arginines provide a strong positive charge; the guanidinium groups (-C(=NH)NH₂) of arginine residues can form strong bidentate hydrogen bonds and electrostatic interactions with heparan sulfate proteoglycans (HSPG) and phospholipid headgroups on the cell membrane surface, which is the key driving force for the efficient cell membrane penetration of polyarginine peptides. The N-terminal Npys (3-nitro-2-pyridinesulfenyl)-activated cysteine can specifically react with another molecule containing a free thiol group to form an asymmetric disulfide bond, achieving site-specific conjugation. C-terminal amidation modification eliminates the negative charge of the C-terminal carboxyl group, increasing the positive charge density of the peptide, while enhancing resistance to carboxypeptidase degradation. Key features and applications of Cys(Npys)-(D-Arg)9: (1) D-amino acid protease resistance - high stability and long half-life in vivo and in serum-containing media; (2) Npys-activated site-specific conjugation - can specifically conjugate to proteins, peptides, nanoparticles, and small molecule drugs containing free thiol groups; (3) intracellular reduction-responsive release - the disulfide bond formed by conjugation is cleaved in the high-glutathione intracellular environment, releasing active cargo; (4) efficient cell penetration - 9 consecutive arginines provide strong cell-penetrating activity; (5) nucleic acid delivery - forming complexes with DNA/siRNA/mRNA to promote gene transfection; (6) protein and peptide delivery - mediating intracellular delivery of functional proteins and peptides; (7) cytotoxicity to microspore cells - studies have shown that this peptide has cytotoxicity to certain cell types and can be used in antitumor research. The Npys group is sensitive to light and reducing agents and should be stored and used under light-protected, reducing-agent-free conditions. |
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) |
| Cys(Npys)-(D-Arg)9 | Npys-modified nona-D-arginine; D-polyarginine conjugation peptide | Cell-penetrating peptide, site-specific chemical conjugation, protease-resistant D-peptide, nucleic acid/drug delivery | Nona-D-arginine N-terminally linked to Npys-modified cysteine; D-arginine sequence resists protease degradation with significantly longer in vivo half-life than L-form, Npys enables site-specific conjugation to thiol carriers, strong positive charge mediates efficient cell penetration | C₆₃H₁₃₀N₃₉O₁₀S₂ | 1677 | ~1678.6 | Acetate | 10 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-DR09-Npys | Yellowish to off-white powder | Store at -20°C, sealed, dry and protected from light, under inert gas. Aliquot for storage. | Stable for 1 month at 2–8°C in sealed dry condition; protect from oxygen and light during shipping. | Stable for 7 days at 4°C. D-form strong cationic peptide is highly soluble in water, dilute acetic acid and acidic buffers. Npys group is sensitive to thiols and reducing agents. D-peptide sequence resists protease degradation with significantly better serum stability than L-form. | Stable for 2 years at -20°C, dry, protected from light and under inert gas. |
Functional Description
| Product Code | Frontend Short Summary (for search list display) | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-DR09-Npys | Npys-modified nona-D-arginine: protease-resistant CPP with site-specific conjugation | Npys-modified nona-D-arginine is a highly stable cell-penetrating peptide. The D-arginine sequence resists in vivo protease degradation, with significantly longer serum half-life and in vivo stability than native L-polyarginine. The strong positively charged sequence efficiently penetrates cell membranes to deliver biomacromolecules, and the N-terminal Npys enables site-specific conjugation to thiol drugs and carriers. | In vivo drug delivery, gene transfection & gene therapy, nanocarrier modification, site-specific chemical conjugation, peptide drug development | Phospholipid bilayer; Npys-thiol conjugation site; electrostatic adsorption transmembrane transport |
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