[Glu2]TRH peptide

[Glu2]TRH peptide

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

Batch to batch variation of the purity

Pyr-EP-NH2

Pyr-Glu-Pro-NH2

2

95.14%

C₁₅H₂₂N₄O₆

354.36

85541-78-2

122148

Synthetic

Powder

[Glu2]TRH is an endogenous peptide with the amino acid sequence pGlu-Glu-Pro-NH2. It is structurally related to thyrotropin-releasing hormone (TRH, pGlu-His-Pro-NH2). [Glu2]TRH is not metabolized by thyroliberinase, an enzyme that rapidly inactivates TRH, and is stable in rat serum for at least 4 hours, being cleared only by the kidneys. [Glu2]TRH does not bind with an appreciable affinity to the two known TRH-receptor isoforms (TRHR1 and TRHR2). [Glu2]TRH possesses intrinsic analeptic activity, but its analeptic action is less efficacious than that of TRH. In mice, it dose-dependently attenuates the TRH-evoked reversal of barbiturate-induced sleeping time. [Glu2]TRH does not possess an intrinsic ACh-stimulatory effect and opposes the cholinergic effect of TRH in the rat CNS. [Glu2]TRH has been reported to have neuroprotective, antidepressant, anticonvulsant, and other activities in the CNS. Many centrally-mediated effects of TRH are shared with [Glu2]TRH, but they may involve different receptors or mechanisms. For example, [Glu2]TRH does not have TSH-releasing activity and does not elevate thyroid-hormone levels. The diastereomer [D-Glu2]TRH is neither an analeptic nor an inhibitor/negative modulator in the context of the analeptic effect and ACh release. [Glu2]TRH may be considered as a negative modulator for the cholinergic effect of TRH in the mouse brain and has the potential to be used as a lead for the development of pharmacological agents to understand the cholinergic mechanisms of TRH's CNS effects.

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

• Nguyen V, Zharikova AD, Prokai-Tatrai K, Prokai L. [Glu2]TRH dose-dependently attenuates TRH-evoked analeptic effect in mice. Brain Res Bull. 2010 Apr 29;82(1-2):83-6. doi: 10.1016/j.brainresbull.2010.02.007. Epub 2010 Feb 24. PMID: 20188155; PMCID: PMC2867048.

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.