BMP-2 mimicking oligo peptide

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

Batch to batch variation of the purity

• SSVPT polypeptide is a BMP - 2 mimicking oligopeptide with significant potential in bone tissue engineering. It can be covalently conjugated to the surface of hydroxyapatite (HA) nanoparticles, which can then be incorporated into poly(methyl methacrylate) (PMMA) bone cement. This modification enhances the bioactivity of the bone cement.
• The presence of SSVPT accelerates the growth of apatite on the cement surface, promotes cell adhesion and proliferation, and increases alkaline phosphatase (ALP) activity, which is an early marker of osteogenic differentiation. It is non - toxic and can synergistically enhance the cytocompatibility of the PMMA - based cement when combined with HA. Overall, SSVPT polypeptide - modified bone cement shows promise as a bioactive biomaterial for weight - bearing bone repair in clinical applications.

• Liu Z, Tang Y, Kang T, Rao M, Li K, Wang Q, Quan C, Zhang C, Jiang Q, Shen H. Synergistic effect of HA and BMP-2 mimicking peptide on the bioactivity of HA/PMMA bone cement. Colloids Surf B Biointerfaces. 2015 Jul 1;131:39-46. doi: 10.1016/j.colsurfb.2015.04.032. Epub 2015 Apr 21. PMID: 25948316.

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.