GV1001 peptide

GV1001 peptide

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

H-EARPALLTSRLRFIPK-OH

H-Glu-Ala-Arg-Pro-Ala-Leu-Leu-Thr-Ser-Arg-Leu-Arg-Phe-Ile-Pro-Lys-OH

16

95.5%

C₈₅H₁₄₆N₂₆O₂₁

1868.22

Synthetic

Powder

GV1001 is a peptide derived from the reverse transcriptase subunit of human telomerase (hTERT). It was originally developed as a vaccine against various cancers. GV1001 exhibits cell-penetrating peptide (CPP) properties, enabling the cytosolic delivery of macromolecules such as proteins, DNA, and siRNA. Unlike typical CPPs, GV1001 achieves cytosolic delivery via interaction with extracellular heat shock protein 90 (eHSP90) and 70 (eHSP70) complexes. The binding of GV1001 to eHSP not only facilitates cytosolic delivery but also leads to additional biological effects. These effects include a strong anti-cancer immune response, potentially contributing to its efficacy as an anticancer vaccine.

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

• Kim JW, Yadav DK, Kim SJ, Lee MY, Park JM, Kim BS, Kim MH, Park HG, Kang KW. Anti-cancer effect of GV1001 for prostate cancer: function as a ligand of GnRHR. Endocr Relat Cancer. 2019 Feb;26(2):147-162. doi: 10.1530/ERC-18-0454. PMID: 30400054.

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.