Hexa-D-arginine peptide

Hexa-D-arginine peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

H-RRRRRR-NH2 (All D-type amino acides)

H-Arg-Arg-Arg-Arg-Arg-Arg-NH2 (All D-type amino acides)

6

95.29%

C₃₆H₇₅N₂₅O₆

954.14

Synthetic

Powder

Hexa-D-arginine is an inhibitor of furin, with Ki values of 106 nM, 580 nM and 13.2 μM for furin, PACE4 and PC1 respectively. Pseudomonas aeruginosa exotoxin A (PEA) protein requires furin-mediated cleavage for manifestation of toxicity and hexa-d-arginine effectively blocks PEA-induced cell lysis and is itself noncytotoxic. Administration of hexa-d-arginine to PEA-treated mice significantly improves their survival rate and decreases circulating levels of tumour necrosis factor alpha. Hexa-D-arginine also blocks furin mediated SARS-CoV-2 spike protein cleavage to suppress virus production and cytopathic effects.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides

• Cameron et al (2000) Polyarginines are potent furin inhibitors. J.Biol.Chem. 275 36741 PMID: 10958789
• Sarac et al (2002) The furin inhibitor hexa-D-arginine blocks the activation of Pseudomonas aeruginosa exotoxin A in vivo. Infect Immun. 70(12) 7136 PMID: 12438396
• Cheng et al (2020) Furin Inhibitors Block SARS-CoV-2 Spike Protein Cleavage to Suppress Virus Production and Cytopathic Effects. Cell Rep. 33(2) 108254 PMID: 33007239

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.