BMP2pp peptide

BMP2pp peptide

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

Batch to batch variation of the purity

H-KIPKASSVPTELSAISTLYL-OH

H-Lys-Ile-Pro-Lys-Ala-Ser-Ser-Val-Pro-Thr-Glu-Leu-Ser-Ala-Ile-Ser-Thr-Leu-Tyr-Leu-OH

20

95.58%

C₉₇H₁₆₄N₂₂O₃₀

2118.46

Synthetic

Powder

BMP2pp is a peptide corresponding to residues 73-92 of the knuckle epitope of bone morphogenetic protein-2 (BMP-2) which inhibits the binding of human recombinant BMP-2 to both BMP receptors type IA and type II. BHP2pp has the same receptor binding capacity and osteogenic properties as the full BMP-2 protein and can promote the formation and regeneration of bone and cartilage, participate in organogenesis, cell differentiation, cell proliferation and apoptosis, but is more stable. In models of artificial joint replacement wear, BMP2pp can ameliorate the Titanium (Ti) mediated impairment in osteogenic potential of human placenta derived mesenchymal stem cells (hPMSCs), suppress the M1 polarization of macrophages through inhibition of the activation of the NF-κB signaling pathway, and ameliorate Ti-induced bone osteolysis.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual: Handling and Storage of Synthetic Peptides

• Saito et al (2003) Activation of osteo-progenitor cells by a novel synthetic peptide derived from the bone morphogenetic protein-2 knuckle epitope. Biochim Biophys Acta 1651(1-2) 60 PMID: 14499589
• Madl (2014) Presentation of BMP-2 mimicking peptides in 3D hydrogels directs cell fate commitment in osteoblasts and mesenchymal stem cells. Biomacromolecules 15(2) 445 PMID: 24400664
• Wang et al (2023) BMP-2 functional polypeptides relieve osteolysis via bi-regulating bone formation and resorption coupled with macrophage polarization. NPJ Regen Med. 8(1) 6 PMID: 36759627

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.