GluR2 (831-842) peptide

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

• Bettler et al (1992) Cloning of a putative glutamate receptor: a low affinity kainate-binding subunit. Neuron 8(2) 257 PMID: 1371217
• Isaac et al (2007) The Role of the GluR2 Subunit in AMPA Receptor Function and Synaptic Plasticity. Neuron 54(6) 859 PMID: 17582328
• Salpietro et al (2019) AMPA receptor GluA2 subunit defects are a cause of neurodevelopmental disorders. Nat Commun 10 3094 PMID: 31300657

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.