TGF-beta1 affinitive peptide

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

Batch to batch variation of the purity

• HSNGLPL peptide is a TGF-β1-binding peptide with unique properties and significant potential in the field of biomaterials and tissue engineering.
• This peptide can be grafted onto polyurethane surface via copper-catalyzed azide–alkyne cycloaddition (CuAAC) click reaction. It plays a crucial role in stabilizing the spatial conformation of TGF-β1 after adhesion. When TGF-β1 adheres to the peptide-grafted polyurethane surface, it forms a loose and diffuse layer, in contrast to the compact and rigid layer on the unmodified polyurethane surface. This indicates that the peptide helps maintain the native structure of TGF-β1, which is beneficial for its bioactivity. The affinitive interaction between HSNGLPL and TGF-β1 also slows down the adsorption process of TGF-β1 on the surface. In vivo animal experiments have shown that the peptide-modified polyurethane with TGF-β1 adsorbed elicits earlier immune reactions and tissue regenerations compared to the unmodified polyurethane, confirming that the peptide can preserve the bioactivity of TGF-β1 on the polymer surface. Overall, HSNGLPL peptide offers a promising approach for improving the performance of biomaterials in tissue engineering applications by enhancing the stability and bioactivity of growth factors like TGF-β1.

• Xiao M, Xiao J, Wu G, Ke Y, Fang L, Deng C, Liao H. Anchoring TGF-β1 on biomaterial surface via affinitive interactions: Effects on spatial structures and bioactivity. Colloids Surf B Biointerfaces. 2018 Jun 1;166:254-261. doi: 10.1016/j.colsurfb.2018.02.059. Epub 2018 Feb 28. PMID: 29602080.

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.