T2 peptide

T2 peptide

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

H-LVGVFH-OH

H-Leu-Val-Gly-Val-Phe-His-OH

6

95.47%

C₃₃H₅₀N₈O₇

670.8

Synthetic

Powder

The T2 peptide (LVGVFH) is a novel peptide that has been identified through screening a phage display peptide library. It has been found to enhance the penetration of bacteriophages across porcine and mouse skin, as well as the penetration of hydrophilic drug molecules such as 5-fluorouracil (5-FU). The T2 peptide interacts with skin lipids to enhance skin penetration, without altering the skin integrity or causing any gross changes in skin morphology. It has been observed that the T2 peptide enhances the partitioning of small molecules with different lipophilicities into the skin, suggesting its potential as a safe and noninvasive peptide for improving the skin penetration of drugs. The T2 peptide has been found to be critical for skin penetration enhancement, with histidine at the c-terminus of the peptide playing a key role.

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

• Kumar S, Sahdev P, Perumal O, Tummala H. Identification of a novel skin penetration enhancement peptide by phage display peptide library screening. Mol Pharm. 2012 May 7;9(5):1320-30. doi: 10.1021/mp200594z. Epub 2012 Apr 16. PMID: 22452335.

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.