Gap 27 peptide

Gap 27 peptide

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

H-SRPTEKTIFII-OH

H-Ser-Arg-Pro-Thr-Glu-Lys-Thr-Ile-Phe-Ile-Ile-OH

11

95.15%

C₆₀H₁₀₁N₁₅O₁₇

1304.53

Synthetic

Powder

Gap 27 is a connexin mimetic peptide corresponding to the SRPTEKTIFFI sequence (amino acids 204–214) on the second extracellular loop of connexin43 (Cx43) which is a selective and reversible inhibitor of Cx43 mediated cell–cell communication, which does not influence Cx43 expression levels. Gap27 effectively inhibits gap junction coupling at concentrations of 50 μM in keratinocytes and HeLa43 cells and is a versatile inhibitor of connexin mediated communication in tissue networks, having been used to identify the role of connexins in cardiomyocyte activities and in pathological processes such as epilepsy.

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

• Ko et al (2000) Biochemical and functional characterization of intercellular adhesion and gap junctions in fibroblasts. Am.J.Physiol.Cell Physiol. 279 C147 PMID: 10898726
• Pollok et al (2011), Connexin 43 mimetic peptide Gap27 reveals potential differences in the role of Cx43 in wound repair between diabetic and non-diabetic cells. J. Cellular Molecular Medicine 15 861 PMID: 20345849
• Faniku et al (2018) The Connexin Mimetic Peptide Gap27 and Cx43-Knockdown Reveal Differential Roles for Connexin43 in Wound Closure Events in Skin Model Systems. International J. Molecular Sciences 19(2) 604 PMID: 29463027

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.