self-assembling P11-4 peptide

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

Batch to batch variation of the purity

• QQRFEWEFEQQ polypeptide is a rationally designed self-assembling peptide. This polypeptide is known for its ability to form β-sheet complexes and self-assemble into 3-dimensional fibrillar scaffolds. It can interact with collagen type I fibers, as demonstrated by atomic force microscopy and surface plasmon resonance analyses. The interaction leads to an increase in the width of collagen fibers, which in turn may enhance the resistance of collagen to proteolysis.
• QQRFEWEFEQQ polypeptide also shows promise in dental applications, such as improving the microtensile bonding strength of the bonding interface to artificial caries-affected dentin and decreasing proteolytic activity. It has the potential to contribute to the formation of a more stable hybrid layer with reduced porosity. Overall, this polypeptide offers interesting possibilities for various biomedical and dental applications.

• de Sousa JP, Carvalho RG, Barbosa-Martins LF, Torquato RJS, Mugnol KCU, Nascimento FD, Tersariol ILS, Puppin-Rontani RM. The Self-Assembling Peptide P11-4 Prevents Collagen Proteolysis in Dentin. J Dent Res. 2019 Mar;98(3):347-354. doi: 10.1177/0022034518817351. Epub 2019 Jan 5. PMID: 30612505.

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.