KL-7 peptide

KL-7 peptide

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

Ac-KLVFFAL-NH2

Ac-Lys-Leu-Val-Phe-Phe-Ala-Leu-NH2

7

95.98%

C₄₆H₇₁N₉O₈

878.11

Synthetic

Powder

KL-7 is a heptapeptide, specifically Ac-KLVFFAL-NH2, that self-assembles into homogeneous peptide nanotubes at neutral pH. The nanotubes have a well-defined nanostructure, with an average length of a few micrometers and a diameter of 30-40 nm. The amino group of the lysine residue in KL-7 is exposed on the nanotube surface. The exposed amino group can react with carbon dioxide, resulting in the formation of carbamate and selective chemisorption of carbon dioxide. The KL-7 nanotube powder has good regeneration properties and is effective in the presence of water. The KL-7 nanotube is suitable for practical applications due to its mild regeneration temperature, low energy consumption requirements, and simple production process.

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

• Geng R , Lu D , Lai Y , Wu S , Xu Z , Zhang W . Peptide nanotube for carbon dioxide chemisorption with regeneration properties and water compatibility. Chem Commun (Camb). 2019 Mar 26;55(26):3797-3800. doi: 10.1039/c9cc00495e. PMID: 30865202.

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.