EGFRvIII peptide

EGFRvIII peptide

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

H-LEEKKGNYV-OH

H-Leu-Glu-Glu-Lys-Lys-Gly-Asn-Tyr-Val-OH

9

95.28%

C₄₈H₇₈N₁₂O₁₆

1079.2

Synthetic

Powder

EGFRvIII peptide is a peptide derived from the fusion junction of epidermal growth factor receptor variant III (EGFRvIII), a variant of EGFR with amino acids 6–273 deleted. This spontaneously occurring alteration is found in a high percentage of primary human brain, breast, lung and ovarian tumours making EGFRvIII an ideal target of immunotherapy in EGFRvIII-expressing tumours. EGFRvIII peptide was identified from a number of candidates as the most immunogenic epitope for major histocompatibility complex I (MHC I) binding to induce tumour specific immune responses. In a glioblastoma mouse brain tumour model EGFRvIII peptide co-administered with the toll-like receptor 5 (TLR5) adjuvant Flagellin B induces an increase in CD8 + T cells and a decrease in Treg cells, inducing tumour apoptosis, inhibiting tumour growth and increasing survival.

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

• Moscatello et al (1997) A naturally occurring mutant human epidermal growth factor receptor as a target for peptide vaccine immunotherapy of tumors. Cancer Res. 57(8) 1419 PMID: 9108438
• Wu et al (2006) Identification of EGFRvIII-derived CTL epitopes restricted by HLA A0201 for dendritic cell based immunotherapy of gliomas. J Neurooncol. 76(1) 23 PMID: 16155724
• Choi et al (2022) Flagellin synergistically enhances anti-tumor effect of EGFRvIII peptide in a glioblastoma-bearing mouse brain tumor model. BMC Cancer 22(1) 986 PMID: 36109710

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.