GPQGIWGQK peptide

GPQGIWGQK peptide

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

H-GPQGIWGQK-OH

H-Gly-Pro-Gln-Gly-Ile-Trp-Gly-Gln-Lys-OH

9

95.43%

C₄₄H₆₇N₁₃O₁₂

970.08

Synthetic

Powder

GPQGIWGQK is a proteolytically cleavable peptide used in the synthesis of bioartificial hydrogel matrices for therapeutic vascularization. It is reacted with acrylate-PEG 3400 -NHS to synthesize MMP-degradable PEGDA macromer (A-PEG-GPQ-PEG-A). The A-PEG-GPQ-PEG-A hydrogel matrix, containing the GPQGIWGQK peptide, exhibits degradation-dependent VEGF release and supports cell adhesion activities. The hydrogel matrix with GPQGIWGQK peptide promotes subcutaneous vessel growth in rats, showing potential for vascularization in tissue engineering applications. The GPQGIWGQK peptide, when incorporated into the hydrogel matrix, allows for controlled release of VEGF, which is important for promoting angiogenesis and tissue regeneration. The bioartificial matrices containing GPQGIWGQK peptide have shown promise in promoting vascularization and could have potential applications in regenerative medicine and tissue engineering.

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

• Phelps EA, Landázuri N, Thulé PM, Taylor WR, García AJ. Bioartificial matrices for therapeutic vascularization. Proc Natl Acad Sci U S A. 2010 Feb 23;107(8):3323-8. doi: 10.1073/pnas.0905447107. Epub 2009 Dec 31. PMID: 20080569; PMCID: PMC2840448.

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.