Synstatin peptide

Synstatin peptide

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

Batch to batch variation of the purity

H-LPAGEKPEEGEPVLHVEAEPGFTARDKE-OH

H-Leu-Pro-Ala-Gly-Glu-Lys-Pro-Glu-Glu-Gly-Glu-Pro-Val-Leu-His-Val-Glu-Ala-Glu-Pro-Gly-Phe-Thr-Ala-Arg-Asp-Lys-Glu-OH

28

95.33%

C₁₃₃H₂₀₇N₃₅O₄₆

3032.26

Synthetic

Powder

Synstatin is a peptide derived from amino acids 92-119 of the mouse syndecan sequence and is the active site for the αvβ3 and αvβ5 integrin activation mechanism. Syndecan is a critical regulator of these two integrins during angiogenesis and tumourigenesis, and this activation process can be blocked by the synstatin peptide. Synstatin displays an IC50 of 100-300 nM when used in vitro to inhibit αvβ3 dependent adhesion and cell migration on vitronectin or in aortic ring angiogenesis assays. Synstatin is a potent inhibitor of angiogenesis in vivo and blocks αvβ3 mediated tumour cell adhesion and migration and tumour formation in mouse models.

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

• Beauvais et al (2009) Syndecan-1 regulates alphavbeta3 and alphavbeta5 integrin activation during angiogenesis and is blocked by synstatin, a novel peptide inhibitor. J Exp Med. 206(3) 691 PMID: 19255147
• Rapraeger (2013) Synstatin: a selective inhibitor of the syndecan-1-coupled IGF1R-αvβ3 integrin complex in tumorigenesis and angiogenesis. FEBS J. 280(10) 2207 PMID: 23375101

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.