slowly degraded matrix metalloprotease (MMP) susceptible peptide

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

Batch to batch variation of the purity

• GPQGIWGQ polypeptide has shown great potential in the field of biomaterials. It can be incorporated into hydrogels, where it plays a crucial role in their formation and functionality. For example, in some hydrogel systems, it serves as a crosslinker, enabling the creation of a three-dimensional network structure. This network provides a stable yet adaptable environment for various biological applications.
• Moreover, GPQGIWGQ is protease-sensitive, specifically to matrix metalloproteinases (MMPs). This property allows for controlled degradation of the materials it is incorporated into, which is vital in processes such as tissue remodeling. When used in combination with other components, such as in certain peptide amphiphile (PA) designs, it can enhance the enzymatic degradation of self-assembling membranes. This makes it a valuable candidate for applications where dynamic and responsive materials are required, such as in wound healing and tissue engineering, where the ability to mimic the natural degradation process of the extracellular matrix is essential for promoting cellular activities and tissue regeneration.

• Vigen M, Ceccarelli J, Putnam AJ. Protease-sensitive PEG hydrogels regulate vascularization in vitro and in vivo. Macromol Biosci. 2014 Oct;14(10):1368-79. doi: 10.1002/mabi.201400161. Epub 2014 Jun 18. PMID: 24943402; PMCID: PMC4198447.

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.