CRGDS peptide

CRGDS peptide

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

H-CRGDS-OH

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

5

95.56%

C₁₈H₃₂N₈O₉S

536.56

Synthetic

Powder

CRGDS forms the cell-binding domain of a glycoprotein, Osteopontin (OPN). 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 its attachment properties. This cleavage occurs within residues of the CRGDS sequence raising the possibility of thrombin-cleavage further activating OPN by allowing greater accessibility of the CRGDS domain to cell surface receptors. CRGDS 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 the 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

• Nguyen EH, Zanotelli MR, Schwartz MP, Murphy WL. Differential effects of cell adhesion, modulus and VEGFR-2 inhibition on capillary network formation in synthetic hydrogel arrays. Biomaterials. 2014 Feb;35(7):2149-61. doi:10.1016/j.biomaterials.2013.11.054. Epub 2013 Dec 11. PMID:24332391; PMCID: PMC3970236.

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.