GRGDS peptide

GRGDS peptide

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

H-GRGDS-OH

H-Gly-Arg-Gly-Asp-Ser-OH

5

95%

C₁₇H₃₀N₈O₉

490.46

Synthetic

Powder

GRGDS is the cell adhesion sequence of osteopontin that recognizes the avb3 integrin. Osteopontin is overexpressed in experimental models of malignancy. Although the native form of OPN is active in cell attachment assays, it has been observed that thrombin cleavage of OPN causes substantial enhancement of it's attachment properties. This cleavage occurs within residues of the GRGDS sequence raising the possibility of thrombin-cleavage further activating OPN by allowing greater accessibility of the GRGDS domain to cell surface receptors. GRGDS synthetic peptide also mimics the cellular binding site of many adhesive proteins in the extracellular matrix and causes rounding and detachment of spread cells. It induces dissociation of alpha-actinin and vinculin from the sites of focal contacts.

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

• Senger DR, Perruzzi CA. Cell migration promoted by a potent GRGDS-containing thrombin-cleavage fragment of osteopontin. Biochim Biophys Acta. 1996 Nov 8;1314(1-2):13-24. doi: 10.1016/s0167-4889(96)00067-5. PMID: 8972713.

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.