Insulin-like growth factor 1 tripeptide, IGF-I (1-3)

Insulin-like growth factor 1 tripeptide, IGF-I (1-3)

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

Batch to batch variation of the purity

GPE

Gly-Pro-Glu

3

99.66%

C₁₂H₁₉N₃O₆

301.3

Synthetic

Powder

This N-terminal tripeptide of IGF-I facilitated the in vitro release of acetylcholine with a several hundredfold higher potency (10⁻¹⁰ - 10⁻⁶ M) than intact IGF-I (4 · 10⁻⁸ M), whereas truncated IGF-I lacking the tripeptide GPE, did not show any significant effect. This raises the possibility that GPE may be the active site of IGF-I. - Although the precise mode of action of GPE is still unknown, another study suggests that local administration of GPE is neuroprotective after brain HI injury via glial cells. In addition, systemic administration of GPE showed a more widespread neuroprotective effect. Therefore, GPE may represent a complementary pathway for central and systemic IGF-1's antiapoptotic 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

• Sara VR, Carlsson-skwirut C, Bergman T, et al. Identification of Gly-Pro-Glu (GPE), the aminoterminal tripeptide of insulin-like growth factor 1 which is truncated in brain, as a novel neuroactive peptide. Biochem Biophys Res Commun. 1989;165(2):766-71.

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.