Ac-IEAR-pNA peptide

Ac-IEAR-pNA peptide

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

Batch to batch variation of the purity

Ac-IEAR-pNA

Ac-Ile-Glu-Ala-Arg-pNA

4

95.08%

C₂₈H₄₃N₉O₉

649.69

Synthetic

Powder

Ac-IEAR-pNA is a cholinesterase inhibitor that is used in the laboratory to measure the activity of butyrylcholinesterase. The enzyme hydrolyzes acetylcholine into butyrylcholine and acetic acid. Ac-IEAR-pNA is a yellow solid with a melting point of about 60°C and an average molecular weight of 288 Da. The enzyme has a Km value of 1.1 mM potassium phosphate, and its catalytic activity increases with increasing concentrations of potassium phosphate, reaching a maximum at 3 mM phosphates. Ac-IEAR-pNA has been shown to be effective in catalytic hydrolysis reactions, which may be due to its ability to bind to the active site of butyrylcholinesterase.

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

• Brawner A, Hinrichs SH, Larson MA, Lockridge O. Heat pretreatment eliminates spurious butyrylcholinesterase enhancement of endotoxin levels in the kinetic chromogenic assay. Chem Biol Interact. 2016 Apr 5;249:19-22. doi: 10.1016/j.cbi.2016.02.015. Epub 2016 Feb 23. PMID: 26915974.

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.