angiopoietin-1 derived peptide

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

Batch to batch variation of the purity

• QHREDG polypeptide is a peptide fragment derived from the growth factor Ang1(angiopoietin-1). It has shown potential in promoting cell survival and adhesion in various cell types.
• This polypeptide can interact with integrin receptors, specifically β1-integrins, which play a crucial role in cell-extracellular matrix interactions. By binding to these receptors, QHREDG polypeptide may activate intracellular signaling pathways that lead to increased cell survival and adhesion. It has been demonstrated to enhance the survival of neonatal rat cardiomyocytes and endothelial cells, and may also have applications in promoting the survival and adhesion of other cell types.
• Overall, QHREDG polypeptide holds promise as a tool for cell culture and tissue engineering applications, with the potential to improve cell viability and function.

• Dang LT, Feric NT, Laschinger C, Chang WY, Zhang B, Wood GA, Stanford WL, Radisic M. Inhibition of apoptosis in human induced pluripotent stem cells during expansion in a defined culture using angiopoietin-1 derived peptide QHREDGS. Biomaterials. 2014 Sep;35(27):7786-99. doi: 10.1016/j.biomaterials.2014.05.018. Epub 2014 Jun 13. PMID: 24930852; PMCID: PMC4117357.

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.