BMP-7 derived peptide

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

Batch to batch variation of the purity

• KPSSAPTQLN peptide is a short peptide derived from bone morphogenetic protein - 7 (BMP - 7). It has a length of 10 amino acids (101–110 amino acid residue sequence of BMP - 7).
• This peptide plays a significant role in promoting osteoblast functions. In vitro studies have shown that when osteoblasts were cultured in the presence of this peptide, their density increased notably after 5 days, and they exhibited a more spread and larger average size morphology after 1 and 3 days of culture compared to controls. Additionally, it was found that peptide combinations involving KPSSAPTQLN, such as the combination with SNVILKKYRN, further enhanced osteoblast proliferation. The peptide also showed potential in enhancing total collagen content in osteoblasts after 21 days of culture. Overall, KPSSAPTQLN peptide holds great promise for applications in bone regeneration and orthopedic biomaterials, as it can effectively stimulate osteoblast activities and contribute to improved bone growth and repair processes. It may be used in the development of novel biomaterials or drug delivery systems to enhance the osseointegration of implants and promote better outcomes in orthopedic treatments.

• Chen Y, Webster TJ. Increased osteoblast functions in the presence of BMP-7 short peptides for nanostructured biomaterial applications. J Biomed Mater Res A. 2009 Oct;91(1):296-304. doi: 10.1002/jbm.a.32246. PMID: 18980196; PMCID: PMC2732755.

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.