F8K peptide

F8K peptide

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

H-FEFKFEFKK-OH

H-Phe-Glu-Phe-Lys-Phe-Glu-Phe-Lys-Lys-OH

9

95.03%

C₆₄H₈₈N₁₂O₁₄

1249.45

Synthetic

Powder

F8K is a peptide sequence designed to self-assemble into a β-sheet nanofiber structure, forming a peptide hydrogel. It is one of the self-assembling peptide hydrogels (SAPHs) that have shown promise in supporting the culture of various cell lineages for stem cell culture and tissue engineering applications. F8K is composed of the amino acids phenylalanine (F), glutamic acid (E), and lysine (K). It has a medium net positive charge at pH 7, with a net charge of 1. F8K has been found to have improved RNA-peptide fibril interactions compared to the neutral peptide F8, suggesting that it facilitates RNA binding to the matrix. However, F8K is not so positively charged that it is prevented from filtering through the spin column, unlike other peptides such as FK and KF8K.

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

• Chiesa I, Ligorio C, Bonatti AF, De Acutis A, Smith AM, Saiani A, Vozzi G, De Maria C. Modeling the Three-Dimensional Bioprinting Process of β-Sheet Self-Assembling Peptide Hydrogel Scaffolds. Front Med Technol. 2020 Oct 15;2:571626. doi: 10.3389/fmedt.2020.571626. PMID: 35047879; PMCID: PMC8757771.

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.