IGF-1bsn peptide

IGF-1bsn peptide

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

Batch to batch variation of the purity

Nap-FFGGYGSSSRRAPQT

1-Nap-Phe-Phe-Gly-Gly-Tyr-Gly-Ser-Ser-Ser-Arg-Arg-Ala-Pro-Gln-Thr-OH

15

95.45%

C₈₃H₁₁₂N₂₂O₂₃

1785.91

Synthetic

Powder

The peptide IGF-1bsn (Insulin-like growth factor-1 bioactive supramolecular nanofiber) is a novel biomaterial. It is obtained by covalently linking dodecapeptides (GYGSSSRRAPQT), which are a key binding site of IGF-1 receptor (IGF-1R) and play an important role in regulating IGF-1 activity, to an assembly peptide, Nap-FFG. IGF-1bsn has the potential to self-assemble and can form an opaque hydrogel by the heating-cooling process in PBS buffer (pH 7.4) at a concentration of 1 mmol/L.
The microstructure of IGF-1bsn is a three-dimensional network composed of nanofibers with a diameter of approximately 20 nm, and Fourier transform infrared spectroscopy shows the characteristic peaks of an amide I band at 1638 cm⁻¹ and an amide III absorption band at approximately 1232 cm⁻¹, corresponding to hydrogen-bonded β-sheet secondary structures.
IGF-1bsn exhibits good stability under physiological conditions and has weak frequency dependence, with the storage modulus (G′) being approximately an order of magnitude higher than the loss modulus (G″). In vitro degradation shows that IGF-1bsn remains above 26% after 24 h.
In rabbit BMSCs experiments, IGF-1bsn promotes BMSC proliferation in a mild and slow manner, enhances the migration of BMSCs at a concentration of 200 nM in vitro, and inhibits BMSC apoptosis. The optimal range to promote cell proliferation and migration, and to inhibit cell apoptosis is 100-200 nM, and 100 times of this concentration (10 μM) is used in subsequent in vivo experiments.
In summary, IGF-1bsn has good stability, biological activity, and the potential to enhance the activity of BMSCs, playing a role in osteogenic / chondrogenic differentiation of BMSCs to improve osteochondral healing and gap space integration after AOT mosaicplasty.

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

• Wu H, Shang Y, Sun W, Ouyang X, Zhou W, Lu J, Yang S, Wei W, Yao X, Wang X, Zhang X, Chen Y, He Q, Yang Z, Ouyang H. Seamless and early gap healing of osteochondral defects by autologous mosaicplasty combined with bioactive supramolecular nanofiber-enabled gelatin methacryloyl (BSN-GelMA) hydrogel. Bioact Mater. 2022 Apr 5;19:88-102. doi: 10.1016/j.bioactmat.2022.03.038. PMID: 35441114; PMCID: PMC9005961.

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.