Biotin-^DFYIGSRGD peptide

Biotin-^DFYIGSRGD peptide

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

Batch to batch variation of the purity

Biotin-fYIGSRGD-OH, f=D-phenylalanine

Biotin-D-Phe-Tyr-Ile-Gly-Ser-Arg-Gly-Asp-OH

8

95.4%

C₅₁H₇₃N₁₃O₁₅S

1140.26

Synthetic

Powder

Biotin-FYIGSRGD (F=D-phenylalanine) could self-assemble into supramolecular hydrogels (termed SupraGel) for 3D cell culture. The introduction of one D-amino acid in the peptide may decrease cell-matrix interactions, thus facilitating spontaneous cell spheroid formation. The pentapeptide YIGSR is from the functional motif (929–933 sequence of the β1 chain) of laminin, a major glycoprotein located in the basement membrane. It can directly bind to the 67 kDa laminin receptor, a non-integrin cell surface receptor, and regulate cell adhesion, growth, differentiation, and migration. The tripeptide arginine-glycine-aspartate (RGD) is a functional motif that binds to the cell surface receptor integrin and regulates cell behavior.

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

• Ai, S., Li, H., Zheng, H. et al. A SupraGel for efficient production of cell spheroids. Sci. China Mater. 65, 1655-1661 (2022). https://doi.org/10.1007/s40843-021-1951-x

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.