RICK peptide

RICK peptide

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

H-kwllrwlsrllrwlarwlg-OH(All D-type amino acids)

H-D-Lys-D-Trp-D-Leu-D-Leu-D-Arg-D-Trp-D-Leu-D-Ser-D-Arg-D-Leu-D-Leu-D-Arg-D-Trp-D-Leu-D-Ala-D-Arg-D-Trp-D-Leu-Gly-OH

19

95.2%

C₁₂₄H₁₉₂N₃₆O₂₁

2523.07

Synthetic

Powder

RICK peptide is a new cell-penetrating peptide which is the retro-inverso form of the CADY-K peptide(sequence: GLWRALWRLLRSLWRLLWK). RICK conserves the main biophysical features of its L-parental homologue and keeps the ability to associate with siRNA in stable peptide-based nanoparticles. Moreover the RICK:siRNA self-assembly prevents siRNA degradation and induces inhibition of gene expression. RICK-based nanoparticles have the same biophysical properties (structure, size, ZP etc.) and the same biological in vitro efficiency (siRNA-induced knock-down) in serum-free or serum containing medium. However, RICK-based nanoparticles have the outstanding property to avoid siRNA degradation based on its own proteolytic stability as demonstrated by pre-incubation with trypsin and serum.

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

• Vaissière A, Aldrian G, Konate K, Lindberg MF, Jourdan C, Telmar A, et al. A retro-inverso cell-penetrating peptide for siRNA delivery. J Nanobiotechnology. 2017;15(1):34

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.