BMP-2 wrist epitope active motif peptide

BMP-2 wrist epitope active motif peptide

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

Batch to batch variation of the purity

H-DWIVA-OH

H-Asp-Trp-Ile-Val-Ala-OH

5

95.8%

C₂₉H₄₂N₆O₈

602.68

Synthetic

Powder

DWIVA polypeptide is a highly promising biomaterial designed for bone regeneration applications. It is a peptide mimic of the active motif in the wrist epitope of bone morphogenetic protein 2 (BMP - 2), possessing high receptor - binding activity and specificity to BMP - receptor types I and II. This unique property enables it to effectively induce osteogenic differentiation. The polypeptide can be easily synthesized and tethered to various biomaterials, offering a cost - effective alternative to traditional growth factors. DWIVA - functionalized hydrogels have shown enhanced osteogenic effects in vitro, increasing alkaline phosphatase (ALP) expression in mesenchymal stem cells (MSCs) cultured both on 2D surfaces and encapsulated in 3D hydrogels. In vivo studies have demonstrated its ability to locally regenerate trabecular bone, making it a potential therapeutic option for treating osteoporosis and preventing fragility fractures. With its tunable conjugation chemistry, the effective concentration of DWIVA in hydrogels can be precisely controlled. Overall, DWIVA polypeptide holds great potential in the field of bone tissue engineering, providing a novel approach for improving bone density and promoting bone regeneration.

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

• Gultian KA, Gandhi R, DeCesari K, Romiyo V, Kleinbart EP, Martin K, Gentile PM, Kim TWB, Vega SL. Injectable hydrogel with immobilized BMP-2 mimetic peptide for local bone regeneration. Front Biomater Sci. 2022;1:948493. doi: 10.3389/fbiom.2022.948493. Epub 2022 Jul 22. PMID: 37090104; PMCID: PMC10120851.

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.