POG peptide

POG peptide

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

Batch to batch variation of the purity

H-PPG-OH

H-Pro-Pro-Gly-OH

3

95.36%

C₁₂H₁₉N₃O₄

269.3

Synthetic

Powder

POG polypeptide is a novel biomaterial designed for intervertebral disc regeneration. It is incorporated into a peptide amphiphile molecule (Col - PA) by combining with VVAG sequence and a hydrophobic lauryl tail. The resulting Col - PA, when mixed with E - PA, forms nanofibers with a porous network structure and stable mechanical properties. These nanofibers provide a biocompatible environment for cells such as rat mesenchymal stem cells (rMSCs), supporting their growth and proliferation.
In vitro experiments demonstrate that POG - containing nanofibers can induce chondrogenic differentiation of MSCs, as evidenced by increased glycosaminoglycan deposition and Sox9 gene expression. In vivo studies using a rabbit needle puncture model of intervertebral disc degeneration show that the Col - PA/E - PA nanofiber scaffold promotes tissue regeneration, with increased deposition of glycosaminoglycans and collagen and reduced degeneration scores compared to control groups. Overall, POG polypeptide - based scaffolds offer a promising solution for the treatment of intervertebral disc degeneration and related spinal disorders.

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

• Fiala T, Barros EP, Ebert MO, Ruijsenaars E, Riniker S, Wennemers H. Frame Shifts Affect the Stability of Collagen Triple Helices. J Am Chem Soc. 2022 Oct 12;144(40):18642-18649. doi: 10.1021/jacs.2c08727. Epub 2022 Sep 30. PMID: 36179150.
• Uysal O, Arslan E, Gulseren G, Kilinc MC, Dogan I, Ozalp H, Caglar YS, Guler MO, Tekinay AB. Collagen Peptide Presenting Nanofibrous Scaffold for Intervertebral Disc Regeneration. ACS Appl Bio Mater. 2019 Apr 15;2(4):1686-1695. doi: 10.1021/acsabm.9b00062. Epub 2019 Mar 26. PMID: 35026903.

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.