Pentapeptide-59 is a synthetic peptide derived from a part of a sequence (Arg-Arg-Arg-Phe-Val) of sea anemone (Heteractis Crispa) venom protein called APHC1. It is a perfect solution for skin sensitivity, leveraging natural mechanisms to inactivate dermal pain receptors.
APHC1 protein might be a promising target to reduce skin sensitivity by inhibiting the overactivation of the TRPV1 pain receptor. Regardless, the full APHC1 protein is unstable during preparation, and the molecule is too large to penetrate the skin barrier. Moreover, harvesting venom from Heteractis Crispa is not practicable for skincare products.
Therefore, a five-amino acid peptide, Pentapeptide-59, was designed by Mibelle Biochemistry in collaboration with the UK Venomtech Institute, an expert in venom drug discovery. This pentapeptide repeats the amino acid sequence of the active TRPV1 receptor binding site of the sea anemone protein. Another advantage is sustainability, as the synthetic production of the peptide does not require sea anemones.
The ability of Pentapeptide-59 to inhibit TRPV1 pain receptor activation was analyzed in CHO cells that stably express TRPV1 receptors. Cells were irritated with capsaicin, which is a TRPV1 activator, either in the presence or absence of sea anemone Pentapeptide-59. Treatment with the full-length sea anemone protein APHC1 at the same molecular concentration was used as a positive control.Results showed that Pentapeptide-59 treatment inhibited TRPV1 receptor activation by 80%, whereas full-length APHC1 inhibited pain receptor activation by 25%. Therefore, the five-amino acid sea anemone peptide exhibits even better TRPV1 inhibition properties than the full-length protein.
