p28 peptide

p28 peptide

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

Batch to batch variation of the purity

H-LSTAADMQGVVTDGMASGLDKDYLKPDD-OH

H-Leu-Ser-Thr-Ala-Ala-Asp-Met-Gln-Gly-Val-Val-Thr-Asp-Gly-Met-Ala-Ser-Gly-Leu-Asp-Lys-Asp-Tyr-Leu-Lys-Pro-Asp-Asp-OH

28

95.59%

C₁₂₂H₁₉₇N₃₁O₄₇S₂

2914.16

Synthetic

Powder

p28 is an amphipathic, α-helical, cell penetrating peptide composed of amino acids Leu50-Asp77 of azurin, a redox protein secreted from the opportunistic pathogen pseudomonas aeruginosa. p28 is a post translational, multitarget anticancer agent that preferentially enters a wide variety of solid tumour cells. On entry, p28 binds to both wild-type and mutant p53 protein, inhibiting constitutional morphogenic protein 1 (cop1) mediated ubiquitination and proteasomal degradation of p53, increasing levels of p53 which induce cell cycle arrest at G2/M and causing apoptosis that results in tumour cell shrinkage and death.

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

• Mehta et al (2011) A cell penetrating peptide derived from azurin inhibits angiogenesis and tumor growth by inhibiting phosphorylation of VEGFR-2, FAK and Akt. Angiogenesis 14(3) 355 PMID: 21667138
• Yamada et al (2013) p28, a first in class peptide inhibitor of cop1 binding to p53. Br J Cancer. 108(12) 2495 PMID: 23736031
• Yaghoubi et al (2020) p28 Bacterial Peptide, as an Anticancer Agent. Front Oncol. 2020 10 1303 PMID: 32850408

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.