heparin-binding domain peptide

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

Batch to batch variation of the purity

• LRKKLGKA peptide is a heparin-binding domain sequence with unique properties and significant potential in biomedical applications.
• This peptide can be fused to the self-assembling peptide RADA16 to form a novel designer self-assembling peptide. It has a strong binding affinity for heparin, which allows it to bind a wide variety of heparin-binding growth factors, such as VEGF. The designer self-assembling peptide formed by incorporating LRKKLGKA can self-assemble into nanofiber scaffolds under physiological conditions, with the nanofibers having a diameter of around 10 nm. This property makes it suitable for use in tissue engineering applications, particularly in the context of myocardial infarction treatment. When used in combination with VEGF, it enables the sustained delivery of VEGF for at least 1 month. This sustained release pattern is beneficial as it can enhance cardiac function recovery by promoting angiogenesis and preventing cardiomyocyte apoptosis. Overall, LRKKLGKA peptide offers a promising approach for improving the treatment of myocardial infarction and other ischemic diseases by facilitating the targeted and prolonged delivery of growth factors.

• Guo HD, Cui GH, Yang JJ, Wang C, Zhu J, Zhang LS, Jiang J, Shao SJ. Sustained delivery of VEGF from designer self-assembling peptides improves cardiac function after myocardial infarction. Biochem Biophys Res Commun. 2012 Jul 20;424(1):105-11. doi: 10.1016/j.bbrc.2012.06.080. Epub 2012 Jun 22. PMID: 22732415.

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.