FGF2-004 peptide

FGF2-004 peptide

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

H-HFKDPKRLYCK-OH

H-His-Phe-Lys-Asp-Pro-Lys-Arg-Leu-Tyr-Cys-Lys-OH

11

95.43%

C₆₆H₁₀₃N₁₉O₁₅S

1434.7

Synthetic

Powder

FGF2-004 is a specific peptide derived from fibroblast growth factor 2 (FGF2) that has been tested for its ability to support the attachment and proliferation of human pluripotent stem cells (hPSCs) in a defined culture environment. The study found that hPSCs cultured on a culture dish co-immobilized with FGF2-004 peptide and a specific fibronectin-derived peptide (PHSRN-GRGDSP) exhibited descent colony morphology with well-defined margins, comparable to cells cultured on Matrigel. Furthermore, hPSCs cultured on the FGF2-004 peptide combined with the PHSRN-GRGDSP motif expressed the highest levels of pluripotency marker genes, such as SOX2 and REX2, among the tested groups. The results suggest that the immobilization of FGF2-004 peptide, along with the PHSRN-GRGDSP motif, on the culture dish can enhance the attachment, proliferation, and pluripotency of hPSCs, potentially reducing the need for continuous growth factor supplementation in large-scale hPSC culture.

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

• Dayem AA, Won J, Goo HG, Yang GM, Seo DS, Jeon BM, Choi HY, Park SE, Lim KM, Jang SH, Lee SB, Choi SB, Kim K, Kang GH, Yeon GB, Kim DS, Cho SG. The immobilization of fibronectin- and fibroblast growth factor 2-derived peptides on a culture plate supports the attachment and proliferation of human pluripotent stem cells. Stem Cell Res. 2020 Mar;43:101700. doi: 10.1016/j.scr.2020.101700. Epub 2020 Jan 7. PMID: 31981882.

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.