Design of melanogenesis regulatory peptides derived from phycocyanin of the microalgae Spirulina platensis

Abstract

Pigmentation issues are common conditions associated with excessive or insufficient production of melanin. Recently peptides are investigated to discover novel melanogenesis regulators as low molecular weight compounds to regulate skin pigmentation. In this study, an internal library of peptides obtained through in silico enzymatic digestion of phycocyanin from microalgae S. platensis was tested to apprehend their anti-melanogenic effects. Seven peptides were investigated for their inhibitory potential against mushroom and B16-F10 murine tyrosinase enzymes. According to the results, P5 (SPSWY) and P7 (AADQRGKDKCARDIGY) were effective in lowering the activity of mushroom and B16-F10 tyrosinases. P5 was the most potent (IC50 value, 12.1 µM) in mushroom which was followed by P2 (MAACLR, 86.9 µM). Although the peptides were particularly powerful in inhibiting monophenolase activity, only moderate inhibition was observed for diphenolase activity in mushroom tyrosinase assay. Apart from tyrosinase inhibition, P2 and P3 (RCLNGRL) were efficient DPPH radical scavengers at low concentrations (IC50 < 200 µM). In the mammalian assay system, P5 and P7 were noticeably effective to decrease tyrosinase enzyme activity with IC50 values of 48.9 and 34.2 µM, respectively. However, although P4 (RYVTYAVF) was a potent mushroom tyrosinase inhibitor, it increased melanin synthesis up to 3-fold in B16-F10 cells. The results indicate that C-terminal tyrosine residue is important for tyrosinase inhibition. This study shows, for the first time, that microalgae proteins can be regarded as sources for melanogenesis regulation.