PZ-128/P1pal-7 peptide

PZ-128/P1pal-7 peptide

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

Batch to batch variation of the purity

Palmitoyl-KKSRALF-NH2

Palmitoyl-Lys-Lys-Ser-Arg-Ala-Leu-Phe-NH2

7

95.27%

C₅₅H₉₉N₁₃O₉

1086.45

371131-16-7

72187679

Synthetic

Powder

P1pal-7, a cell-penetrating lipopeptide pepducin, is a N-palmitoylated peptide with the sequence C15H31CONH-KKSRALF-NH2. Pepducins are cell-penetrating lipo-peptide conjugates based on the sequences of the intracellular loops of PAR1 and other GPCRs. The lipid moiety of P1pal-7 anchors the compound to the lipid bilayer after delivering its cargo across the plasma membrane, thereby concentrating the pepducin to the target receptor-G protein interface. P1pal-7 was used to block PAR1-dependent migration of ovarian carcinoma cells. It was found that P1pal-7, along with other PAR1-based pepducins such as P1pal-12, strongly inhibited the migration of OVCAR-4 and IGROV-1 ovarian carcinoma cells toward malignant ascites fluid and fibroblast conditioned media. Additionally, P1pal-7 was shown to reduce ascites production and angiogenesis in mouse models of peritoneal ovarian cancer, and when combined with docetaxel, it inhibited the metastatic progression of the cancer. Overall, P1pal-7 provides an in vivo proof-of-concept that targeting the metalloprotease-PAR1 signaling system may be a novel therapeutic approach in the treatment of ovarian cancer.

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

• Agarwal A, Covic L, Sevigny LM, Kaneider NC, Lazarides K, Azabdaftari G, Sharifi S, Kuliopulos A. Targeting a metalloprotease-PAR1 signaling system with cell-penetrating pepducins inhibits angiogenesis, ascites, and progression of ovarian cancer. Mol Cancer Ther. 2008 Sep;7(9):2746-57. doi: 10.1158/1535-7163.MCT-08-0177. PMID: 18790755; PMCID: PMC2735132.

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.