We identified vespid chemotactic peptide (VCP) and vespakinin (Vespk) from the lesser paper wasp, Parapolybia varia . The cDNA, genomic DNA, and mature peptide sequences of P. varia VCP ( Pv VCP) and Vespk ( Pv Vespk) were determined. To investigate the pharmacological and toxicological properties of Pv VCP and Pv Vespk, their hemolytic, anti-microbial, anti-fungal, and anti-tumor activities were evaluated and compared with those of Vespa mandarina VCP ( Vm VCP) and Vespk ( Vm Vespk). Pv VCP, Pv Vespk, and Vm Vespk showed little to low hemolytic activities. Only Vm VCP showed hemolytic activity at a high concentration. Among the four peptides tested, Vm VCP showed both anti-microbial and anti-fungal activities, whereas Pv VCP showed only anti-fungal activity to Candida albicans . Interestingly, Pv VCP showed significantly stronger anti-tumor activities to two ovarian cancer cell lines compared with Vm VCP. Vespks only showed anti-tumor activity to SK-OV-3 cells but not to NIH-OVCAR-3 cells. These differences in anti-tumor activity might have been caused by the differences in secondary structure among peptides. A circular dichroism spectrometry analysis revealed that VCPs have more amphiphilic α-helix structures than Vespks. Taken together, the low hemolytic but strong anti-tumor activities of Pv VCP suggest that this peptide could be a candidate for developing a new anti-tumor peptide drug or drug carrier in the future.
