BMP-7 (121-130) peptide

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

Batch to batch variation of the purity

• SNVILKKYRN peptide is a bioactive peptide derived from bone morphogenetic protein - 7 (BMP - 7). It consists of a specific sequence of amino acids and is designed to potentially interact with osteoblasts, the cells responsible for bone formation.
• This peptide has shown interesting effects in in vitro studies related to bone biology. When combined with another peptide, KPSSAPTQLN, it has the ability to enhance osteoblast density. This suggests that it may play a role in promoting the proliferation of osteoblasts, which is a crucial step in the process of bone growth and repair. Although on its own, it may not have the most significant impact on osteoblast density compared to some other peptides, its combination with other factors appears to have synergistic effects. SNVILKKYRN peptide holds promise as a potential component in strategies aimed at improving bone regeneration, perhaps in the development of novel biomaterials or therapeutic approaches for orthopedic applications where enhancing osteoblast activity is desired. It could potentially be incorporated into systems that aim to mimic the natural processes of bone formation and repair, contributing to better outcomes in bone - related 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.