GRGDTP peptide

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

The GRGDTP peptide is a synthetic oligopeptide containing the Arg-Gly-Asp (RGD) sequence, a well-known recognition motif for integrin receptors. In the context of cellular mechanosensing studies, GRGDTP functions as a competitive inhibitor that specifically disrupts interactions between integrins and extracellular matrix (ECM) proteins bearing the RGD motif, such as fibronectin and vitronectin. Experimental evidence demonstrates that GRGDTP, at a concentration of 100 µg/ml, effectively blocks the mitogenic response and platelet-derived growth factor (PDGF) secretion induced by cyclic mechanical strain in vascular smooth muscle cells. This inhibition is sequence-specific, as the control peptide GRGESP does not produce this effect. The action of GRGDTP highlights the critical role of specific integrin-ECM interactions in transducing mechanical signals into intracellular biochemical responses.

• Wilson E, Sudhir K, Ives HE. Mechanical strain of rat vascular smooth muscle cells is sensed by specific extracellular matrix/integrin interactions. J Clin Invest. 1995 Nov;96(5):2364-72. doi: 10.1172/JCI118293. PMID: 7593624; PMCID: PMC185888.

Trifluoroacetic acid (TFA) is a common counterion from the purification process using High-Performance Liquid Chromatography (HPLC). The presence of TFA can affect the peptide's net weight, appearance, and solubility.

Impact on Net Weight: The TFA salt contributes to the total mass of the product. In most cases, the peptide content constitutes >80% of the total weight, with TFA accounting for the remainder.

Solubility: TFA salts generally enhance the solubility of peptides in aqueous solutions.

In Biological Assays: For most standard in vitro assays, the residual TFA levels do not cause interference. However, for highly sensitive cellular or biochemical studies, please be aware of its presence.