pHLIP peptide

pHLIP peptide

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

Batch to batch variation of the purity

H-AAEQNPIYWARYADWLFTTPLLLLDLALLVDADEGTCG-OH

H-Ala-Ala-Glu-Gln-Asn-Pro-Ile-Tyr-Trp-Ala-Arg-Tyr-Ala-Asp-Trp-Leu-Phe-Thr-Thr-Pro-Leu-Leu-Leu-Leu-Asp-Leu-Ala-Leu-Leu-Val-Asp-Ala-Asp-Glu-Gly-Thr-Cys-Gly-OH

38

95.49%

C₁₉₆H₂₉₃N₄₅O₅₈S

4239.73

Synthetic

Powder

The pH-low insertion peptide (pHLIP) holds great promise for diagnostic and therapeutic applications in diseases characterized by acidosis. Based on environmental factors, pHLIP can assume three different stable states: at neutral pH, pHLIP is unstructured in solution (State I), but in the presence of lipid bilayers it binds to the membrane surface (State II). Finally, a drop in pH causes pHLIP to insert across the membrane and fold into a transmembrane helix (State III). pHLIP has been shown to target different solid tumor types, and to translocate membrane-impermeable drugs across the plasma membrane into the cytoplasm of cancer cells

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

• Reshetnyak YK, Andreev OA, Lehnert U, Engelman DM. Translocation of molecules into cells by pH-dependent insertion of a transmembrane helix. Proc Natl Acad Sci U S A. 2006 Apr 25;103(17):6460-5.
• Scott HL, Westerfield JM, Barrera FN. Determination of the Membrane Translocation pK of the pH-Low Insertion Peptide. Biophys J. 2017 Aug 22;113(4):869-879. doi: 10.1016/j.bpj.2017.06.065. PMID: 28834723; PMCID: PMC5567424.
• Dhuri K, Duran T, Chaudhuri B, Slack FJ, Vikram A, Glazer PM, Bahal R. Head-to-head comparison of in vitro and in vivo efficacy of pHLIP-conjugated anti-seed gamma peptide nucleic acids. Cell Rep Phys Sci. 2023 Oct 18;4(10):101584.
• Li X, Jian M, Sun Y, Zhu Q, Wang Z. The Peptide Functionalized Inorganic Nanoparticles for Cancer-Related Bioanalytical and Biomedical Applications. Molecules. 2021 May 27;26(11):3228.

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.