PE-22-28

PE-22-28 is a synthetic heptapeptide derived from Spadin, an endogenous peptide generated from the maturation of sortilin/NTS3. Within peptide science, PE-22-28 is being studied for its interaction with TREK-1 (KCNK2), a two-pore potassium channel that is central to research on ion channel regulation, neuronal excitability, and signaling modulation. In preclinical models, the peptide is associated with channel-mediated pathway dynamics and molecular binding kinetics (Veyssière J. et al., 2015).

History of PE-22-28

PE-22-28 was developed as an abbreviated Spadin analogue from research on more stable TREK-1 interactors. The original Spadin sequence is derived from the C-terminal pro-sortilin fragment, and abbreviated peptide analogues have been characterized in later studies. PE-22-28 contains the 7-amino acid core sequence (GVSWGLR) that has been shown to be necessary for TREK-1 binding within the investigated models. This optimization represents a progress in the research on peptide-channel interaction studies and molecular stability (Djillani A. et al., 2017).

PE-22-28 Structure and molecular data

Peptide Name: PE-22-28 Peptide Type: Synthetic Heptapeptide Sequence: Gly-Val-Ser-Trp-Gly-Leu-Arg

CAS#: 1801959-12-5 Molecular Formula: C35H55N11O9 Molecular Weight: 773.89 g/mol

The heptapeptide structure is designed for selective interaction with the TREK-1 channel and studied within ion-channel and neurobiological research.

PE-22-28 Research findings

PE-22-28 has been investigated in in-vitro and preclinical models focusing on TREK-1 channel dynamics, neuronal signaling modulation, and peptide channel binding kinetics. Studies describe interaction with two-pore potassium channel systems and characterization within molecular signaling pathways.

Major Research Areas of PE-22-28

Ion Channel

Focus on TREK-1 (KCNK2) interaction, K2P channel dynamics, and binding kinetics.

Neurobiology

Investigation of neuronal excitability, synaptic signaling models and channel-mediated pathways.

Molecular

Study of peptide-protein binding, conformational stability and structure-activity relationship.

Scientific Relevance of PE-22-28

PE-22-28 is considered a relevant research molecule for studies on ion channel regulation and peptide-mediated channel modulation. Through selective interaction with the TREK-1 channel, it provides a tool for studying K2P dynamics in controlled in-vitro research environments.

References

Veyssière J. et al. (2015). Retroinverso analogs of spadin display increased antidepressant effects. Psychopharmacology, 232(3), 561–574. Djillani A. et al. (2017). Shortened Spadin analogs display better TREK-1 inhibition, in vivo stability, and antidepressant activity. Frontiers in Pharmacology, 8, 643. Mazella J. et al. (2010). Spadin, a sortilin-derived peptide, targeting rodent TREK-1 channels. PLoS Biology, 8(4), e1000355.