LAH4-L1 peptide (TFA removed)

LAH4-L1 peptide (TFA removed)

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

H-KKALLAHALHLLALLALHLAHALKKA-NH2

H-Lys-Lys-Ala-Leu-Leu-Ala-His-Ala-Leu-His-Leu-Leu-Ala-Leu-Leu-Ala-Leu-His-Leu-Ala-His-Ala-Leu-Lys-Lys-Ala-NH2

26

95.2%

C₁₃₂H₂₂₉N₃₉O₂₆

2778.47

Synthetic

Powder

LAH4-L1 was identified to be a highly potent nucleic transfection agent while LAH4-A4(KKALLHLALLHAALLAHHLALALKKA-NH2), commonly called vectofusin-1 (VF-1), is very active in enhancing lentiviral transduction. Notably, these two peptides exhibit the same overall composition of amino acids but their distribution along the sequence and three-dimensional structure is different.

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

• Lointier M, Aisenbrey C, Marquette A, Tan JH, Kichler A, Bechinger B. Membrane pore-formation correlates with the hydrophilic angle of histidine-rich amphipathic peptides with multiple biological activities. Biochim Biophys Acta Biomembr. 2020 Aug 1;1862(8):183212. doi: 10.1016/j.bbamem.2020.183212. Epub 2020 Feb 11. PMID: 32057757.

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.