Synthetic peptides inducing metamorphosis in a tropical jellyfish: a quantitative structure-activity relationship study

Synthetic peptides are known to trigger metamorphosis to the polyp stage in larvae and larva-like buds of the jellyfish Cassiopea andromeda. Coupling of a hydrophobic moiety to the amino terminus of such peptides was found to increase their efficiency. Hydrophobicity can thus be considered an important factor in the biological activity of peptidic inducers. By establishing the n-octanol/water partition coefficient in order to characterize the hydrophobicity of bioactive peptides, we demonstrate that this parameter and efficiency are positively correlated in peptides of the same amino acid sequence. Hydrophobicity proved to be of much lesser importance than amino acid sequence when data of structurally disparate inducer peptides were considered.