KKFFVLK peptide

KKFFVLK peptide

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

Batch to batch variation of the purity

H-KKFFVLK-OH

H-Lys-Lys-Phe-Phe-Val-Leu-Lys-OH

7

95.96%

C₄₇H₇₆N₁₀O₈

909.17

Synthetic

Powder

KKFFVLK polypeptide is a peptide amphiphile (PA). This polypeptide contains a hexadecyl lipid chain and a peptide sequence with two phenylalanine (FF) residues at the C-terminus. The FF residues drive self-assembly through hydrophobic and π-stacking interactions. It is designed based on the KLVFF core motif from the amyloid beta (Aβ) peptide. The serine protease α-chymotrypsin can cleave KKFFVLK at two sites, leading to products KKF with FVLK and KKFF with VLK. KKFFVLK forms nanotubes and helical ribbons at room temperature, which is associated with its substantial β-sheet secondary structure. This nanostructure causes light scattering and a partly cloudy appearance in solution. The ability of KKFFVLK to form specific nanostructures and its responsiveness to enzymatic cleavage make it an interesting candidate for applications such as enzyme-responsive delivery systems or in the study of self-assembly processes related to biomaterials and nanotechnology.

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

• Dehsorkhi A, Hamley IW, Seitsonen J, Ruokolainen J. Tuning self-assembled nanostructures through enzymatic degradation of a peptide amphiphile. Langmuir. 2013 Jun 4;29(22):6665-72. doi: 10.1021/la401025r. Epub 2013 May 17. PMID: 23651310; PMCID: PMC3678293.

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.