RP-182 peptide (TFA removed)

RP-182 peptide (TFA removed)

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

H-KFRKAFKRFF-OH

H-Lys-Phe-Arg-Lys-Ala-Phe-Lys-Arg-Phe-Phe-OH

10

95.85%

C₆₉H₁₀₃N₁₉O₁₁

1374.67

Synthetic

Powder

The company Riptide Biosciences (Vallejo, CA, USA) designed a linear peptide that binds to CD206. The peptide, named RP-182 (sequence: KFRKAFKRFF) consists of alternating hydrophobic and hydrophilic aminoacids. Because the peptide also binds to RelB and CD47, the selectivity of systemically administered RP-182 for M2 TAMs remains to be seen. Interestingly, in a congress abstract the peptide was recently reported to induce phagocytosis and apoptosis in M2 mouse macrophages. This activity could be linked to the conformational change of CD206 produced by RP-182.

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

• Sable R., Jaynes J., Ronzetti M., Guzman W., Knotts Z., Val N., de Morgan J., Yates C., Bolormaa B., Rudloff U. Abstract B49: Precision targeting of M2-like macrophages by the innate defense regulator RP-182 in pancreatic cancer and noncancerous diseases. Cancer Res. 2019;79:B49.
• Scodeller, P., Simón-Gracia, L., Kopanchuk, S. et al. Precision Targeting of Tumor Macrophages with a CD206 Binding Peptide. Sci Rep 7, 14655 (2017). https://doi.org/10.1038/s41598-017-14709-x

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.