Phytochelatin 2 peptide

Phytochelatin 2 peptide

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

Batch to batch variation of the purity

γ-Glu-Cys-γ-Glu-Cys-Gly

γ-Glu-Cys-γ-Glu-Cys-Gly

5

97.5%

C₁₈H₂₉N₅O₁₀S₂

539.58

Synthetic

Powder

Phytochelatins (PCs) are a family of thiol-rich peptides, with the general structure (γ-Glu-Cys) n -Gly, with n = 2−11, induced in plants upon exposure to excessive amounts of heavy metals and some metalloids, such as arsenic. Studies with Cd(II), Hg(II), and Pb(II) show that the synthetic (Glu-Cys)2Gly peptide exhibits metal-chelating properties similar to the phytochelatin (γ Glu-Cys)2Gly.

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

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.